Ion channels with improved properties

Abstract

The invention relates to methods of increasing stomatal function in plants, which leads to an increase in water use efficiency and ultimately an increase in biomass and yield. In particular the methods of the invention relate to modifying stomatal voltage-gated potassium channels to accelerate stomatal conductance and kinetics. Also described are plants expressing these modified channels and well as methods of producing such plants.

Description

[0001]Ion channels with improved properties FIELD OF THE INVENTION The invention relates to methods of increasing stomatal function in plants, which leads to an increase in water use efficiency and ultimately an increase in biomass and yield. In particular, the methods of the invention relate to modifying stomatal voltage-gated potassium channels to accelerate stomatal conductance and kinetics. Also described are plants expressing these modified channels and well as methods of producing such plants. BACKGROUND OF THE INVENTION Globally, water usage has increased 6-fold in the past 100 years, twice as fast as the human population, and is expected to double again before 2030, driven mainly by irrigation and agriculture. In the UK alone, irrigation has risen 10-fold in the past 30 years and this trend is expected to continue. Stomata are pores in the leaf epidermis that form between pairs of guard cells. They allow CO2 uptake for photosynthetic carbon assimilation at the expense of water loss via transpiration. As such, they provide the major route for gaseous exchange between the interior of the leaf and the atmosphere and can limit photosynthetic rates by 50% or more when demand exceeds water supply. Stomata exert a major control on the water and carbon cycles of the world, and their activity in crops has been a key factor in global atmospheric modelling and weather prediction for over a quarter of a century. Stomatal aperture is controlled by guard cell turgidity, which responds to changes in atmospheric CO2 concentration, light, atmospheric relative humidity, and abscisic acid, thereby regulating plant water use. To date, efforts to improve plant water use efficiency have focused largely on reducing stomatal density, despite its implicit penalty in carbon assimilation. Approaches that circumvent the carbon:water trade-off pose greater challenges but also provide much promise. In particular, accelerating the kinetics of stomatal opening and closing could be used to promote carbon assimilation under high light intensities, while maintaining plant water status when carbon demand is low. 14051746-1 Much research to date has focused on enhancing water use efficiency (WUE) by reducing stomatal densities, an approach that decreases transpiration but can also reduce CO2 availability for photosynthesis and slow plant growth. Some studies have shown that altering the populations of ion pumps and channels will affect stomatal conductance and photosynthesis, but commonly at the expense either of WUE or of carbon assimilation. There therefore exists a need to accelerate stomatal kinetics to reduce transpiration rates from the stomata without affecting photosynthesis. This will be particularly important in crops with slow stomatal kinetics, and will ultimately lead to an increase in growth and / or yield in these crops. The present invention addresses this need. SUMMARY OF THE INVENTION We have shown that by introducing mutations into stomatal voltage-gated potassium channels, we can alter channel clustering and the voltage- and K+-dependencies for K+flux, thereby enhancing guard cell membrane transport and accelerating stomatal movements. These findings underscore the gains possible by 'tuning' the gating of channels native to the plant to improve WUE and carbon assimilation, thus circumventing the often conflicting demands in conserving water while ensuring photosynthetic assimilation for growth. In one aspect of the invention there is provided a genetically altered plant, plant part or plant cell, wherein the plant is characterised by at least one mutation in a C-linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is not a substitution of glycine at position 313 at SEQ ID NO: 1. In another aspect of the invention there is provided a method of altering the channel kinetics of a stomatal voltage-gated potassium channel, wherein an alteration in channel kinetics is preferably selected from a change in sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage-sensitive ion channel (I), wherein the method comprises introducing at least one 14051746-1 mutation into the C-linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is not a mutation at position 313 of SEQ ID NO: 1 and / or or at least one mutation into the cytosolic N-terminal domain, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal. In another aspect of the invention, there is provided a method of increasing at least one of growth, yield, drought tolerance, water use efficiency and / or carbon assimilation in a plant, wherein the method comprises introducing at least one mutation into the C-linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is not a mutation at position 313 of SEQ ID NO: 1 and / or or at least one mutation into the cytosolic N-terminal domain, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal. In another aspect of the invention there is provided a method of producing a genetically altered plant, part thereof or plant seed, the method comprising introducing at least one mutation into the C-linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is not a mutation at position 313 of SEQ ID NO: 1 and / or or at least one mutation into the cytosolic N-terminal domain, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal. The C-linker domain may comprise at least four alpha-helices, and wherein the at least one mutation is in the first N-terminal alpha helix, the second N-terminal helix or between the first and second alpha helices (as used herein N-terminal means the N-terminus of the C-linker). In one embodiment, the first N-terminal alpha helix comprises a sequence selected from SEQ ID NO: 37 to 39, or a functional variant thereof, wherein the functional variant has at least 60% overall sequence identity to SEQ ID NO: 37 to 39. In another embodiment, the second N-terminal alpha helix comprises a sequence selected from SEQ ID NO: 40 to 42, or a functional variant thereof, wherein the functional variant has at least 60% identity to SEQ ID NO: 40 to 42. The C-terminal helix may also comprise a (K / R)LGR domain, wherein the at least one mutation is within the (K / R)LGR domain. 14051746-1 In one embodiment, the mutation is a substitution of at least one positively charged amino acid for a negatively charged amino acid or a neutral amino acid. On another embodiment, the mutation is a substitution of at least one negatively charged amino acid for a positively charged amino acid or a neutral amino acid. In another embodiment, the mutation is the substitution of a neutral amino acid for a charged (positive or negative) or a residue with a larger mass. In one embodiment, the mutation is at a position selected from at least one of 312, 316, 317, 318, 319, 320, 321, 332, 333, 334, 335, 336, 337, 348, 349, 350, 351, 352 and / or 356 of SEQ ID NO: 1, or corresponding position in a homologous sequence, and wherein the mutation is not at position 313 of SEQ ID NO: 1. In one embodiment, the corresponding position in a homologous sequence is selected from: a. positions 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434 and 435 of SEQ ID NO: 31; or b. positions 352, 356, 357, 358, 359, 360, 361, 372, 373, 374, 375, 376, 377, 388, 389, 390, 391 and 392 of SEQ ID NO: 32 or 33; or c. positions 353, 357, 358, 359, 360, 361, 362, 373, 374, 375, 376, 377, 378, 389, 390, 391, 392 and 393 of SEQ ID NO: 17. Alternatively, the corresponding position in a homologous sequence is selected from: d. positions 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434 and 435 of SEQ ID NO: 34 or 36; or e. positions 264, 268, 269, 270, 271, 272, 273, 284, 285, 286, 287, 288, 289, 300, 301, 302, 303 and 304 of SEQ ID NO: 35. In one embodiment, the mutation is at least two mutations at positions selected from K312, E317, D321 of SEQ ID NO: 1 or at least two corresponding positions in a homologous sequence. In one embodiment, the at least two corresponding positions of a homologous sequence are selected from: a. K395, E400 and D404 of SEQ ID NO: 31; or b. K352, E357 and D361 of SEQ ID NO: 32 or 33; or c. K353, E358 and D362 of SEQ ID NO: 17. 14051746-1 Alternatively, the at least two corresponding positions of a homologous sequence are selected from: d. K329, E334 and D338 of SEQ ID NO: 34 or 36; or e. K264, E269 and D273 of SEQ ID NO: 35. The plant, part thereof or plant cell further comprises at least one mutation in a N-terminal cytosolic domain. In one embodiment, the at least one mutation alters the pattern of charged amino acids in the N-terminal domain. Preferably, the mutation is the substitution of at least one positively charged amino acid for a negatively charged amino acid or a neutral amino acid and / or the mutation is the substitution of at least one negatively charged amino acid for a positively charged amino acid or a neutral amino acid. In another embodiment, the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal domain. In another aspect of the invention there is provided a genetically altered plant, plant part or plant cell, wherein the plant is characterised by at least one mutation in a N-terminal cytosolic domain of a stomatal voltage-gated potassium channel, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal. In one embodiment, the N-terminal domain comprises SEQ ID NO: 55 or a variant thereof. In another aspect of the invention, there is provided a genetically altered plant, plant part or plant cell, wherein the plant is characterised by at least one mutation in a N-terminal cytosolic domain of a stomatal voltage-gated potassium channel, and further at least one mutation in the C-linker domain of a stomatal voltage-gated potassium channel. In one embodiment, the stomatal voltage-gated potassium channel is GORK, and the at least one mutation in the N-terminal cytosolic domain is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the at least one mutation in the C-linker domain is at position 317. 14051746-1 In a preferred embodiment, the stomatal voltage-gated potassium channel comprises a sequence selected from (UniProtKB / Swiss-Prot) accession number Q94A76.2; (GenBank) KAG4383022.1, KAG4402628.1, KAG4402629.1., PWZ19722.1, AAW82753.1, AQK83496.1, or (NCBI) XP_003544361.1. In one embodiment, the homologous sequence is selected from accession number (UniProt) Q94A76.2; (GenBank) KAG4383022.1, KAG4402628.1, KAG4402629.1., PWZ19722.1, AAW82753.1, AQK83496.1, or (NCBI) XP_003544361.1. In one embodiment, the stomatal voltage-gated potassium channel is a GORK channel. Preferably, the GORK channel comprises an amino acid sequence as defined in SEQ ID NO: 1, 3, 5 or a functional variant or homologue thereof. In one embodiment, the genetically altered plant, plant part or plant cell as described herein is a monocot or dicot. In one embodiment, the plant part is a seed. In another aspect of the invention there is provided a nucleic acid construct comprising a nucleic acid sequence encoding a voltage-gated potassium channel comprising at least one mutation in the C-linker domain, wherein the at least one mutation is not at position 313 of SEQ ID NO:1. In one embodiment, the nucleic acid construct comprises a nucleic acid sequence encoding a voltage-gated potassium channel selected from SEQ ID NO: 49, 50, 51, 52, 53 and 54 or a functional variant thereof, wherein the functional variant has at least 60% overall sequence identity to one of SEQ ID NO: 49, 50, 51, 52, 53 and 54, wherein preferably the nucleic acid sequence encoding a voltage-gated potassium channel is operably linked to a regulatory sequence. In another aspect of the invention there is provided an isolated plant cell transfected with at least one nucleic acid construct as defined herein. In another aspect of the invention there is provided the use of a nucleic acid construct as defined herein to increase at least one of growth, yield, drought tolerance, water use efficiency and / or carbon assimilation in a plant. 14051746-1 DESCRIPTION OF THE FIGURES The invention is further described in the following non-limiting figures: Figure 1. GORK K+ channels interact through the cytosolic N-termini of the voltage sensor domains (a) Schematic of Kv channel subunit structure (above) with the six, transmembrane a - helices (S1-S6), intervening loops (L1-L4) and chimera exchange points indicated. Four homologous subunits assemble around a central pore to give a functional channel with the voltage-sensor domains (VSDs) forming an outer ring within the plane of the membrane. Neighbouring channels may come together bridged by interactions between VSDs, but interactions between subunits will also occur between individual subunits within the channel assembly. Exploring interactions between VSDs therefore requires to isolate one VSD component. (b) Selective binding occurs between GORK and the GORK VSD (gVSD) but is not evident with either KAT1 or its VSD (kVSD). Cartoons (left) indicate the bait and prey structures. One of three independent experiments, all yielding similar results. Yeast mating-based split-ubiquitin assay for interaction of the Nub-X channel and VSD fusions, including controls ([-], NubG; [+], NubI), with the GORK-Cub bait fusion. Yeast diploids dropped at 1.0 and 0.1 OD600 spotted (left to right) on complete synthetic medium without Trp, Leu, Ura and Met (CSM-LTUM) to verify mating, on CSM without Trp, Leu, Ura, Ade, His and Met (CSM-LTUMAH) to verify adenine- and histidine-independent growth, and with Met additions to suppress bait expression. (c) Chimeras of the GORK VSD (gVSD) and KAT1 VSD (kVSD) interact with the full-length GORK channel provided the VSD prey includes the gVSD N-terminus. Cartoons (left) indicate the bait and prey structures. One of three independent experiments, all yielding similar results. Yeast mating-based split-ubiquitin assay for interaction of the Nub-X VSD and VSD chimera fusions, including controls ([-], NubG; [+], NubI), with the GORK-Cub bait fusion as in (b). Figure 2. Alternation of charges defines GORK VSD interactions Mutation of the GORK VSD N-terminus supports interaction provided the alternation of charges is retained. (a) Alignment of the N-terminal cytosolic domains GORK homologs highlights an alternation of positive and negative charged regions. Sequences (NCBI 14051746-1 identifiers) from Arabidopsis thaliana (CAC17380.1), Brassica napus (XP_013656069.1), Arabidopsis relative Tarenaya hassleriana (XP_010553885.1), oil palm Elaeis guineensis (XP_010905454.2), pepper Capsicum annuum (KAF3658364.1), wheat Triticum aestivum (XP_044442180.1), and rice Oriza sativa (XP_015644419.1). Charged residues (positive, blue; negative, yellow) are highlighted. (b) Alignment of the GORK and KAT1 N-termini. Negative and positive charged residues were exchanged in gVSDPNand gVSDNP, respectively, and are substituted with Ala in gVSDA. His residues were included as these carry a substantial positive charge at neutral pH. All charged residues were exchanged in gVSDPNNP. (c) One of three independent experiments, all yielding similar results testing the residue mutants in (b) for interaction with the full-length GORK channel here cross-referenced by color coding (left). Yeast mating-based split-ubiquitin assay for interaction of the Nub-X VSD fusions, including controls ([-], NubG; [+], NubI), with the GORK-Cub bait fusion. Yeast diploids dropped at 1.0 and 0.1 OD600 spotted (left to right) on complete synthetic medium without Trp, Leu, Ura and Met (CSM-LTUM) to verify mating, on CSM without Trp, Leu, Ura, Ade, His and Met (CSM-LTUMAH) to verify adenine- and histidine-independent growth, and with Met additions to suppress bait expression. Figure 3. Non-interacting channel mutations suppress GORK clustering when stably expressed in Arabidopsis (a) Confocal analysis of GFP channel fusions (GFP), chlorophyll fluorescence (Chlpst), and corresponding brightfield (Bright) images from gork Arabidopsis leaf epidermis transformed with wild-type GORK-GFP (GORKwt), GFP fusions of the non-interacting mutations GORKkN-gS1-L4and GORKNP, and the interacting GORKPNNPmutant under control of the guard cell pGC1 promoter. Representative image sets from leaves infiltrated with 0.1 mM and subsequently with 50 mM K+. Scale bar, 10 µm. (b) Relative standard deviation (RSD) of GFP distributions. RSD calculated from the GFP fluorescence measured along a 2 µm-wide line traced over the periphery of 10 guard cells selected at random in n>6 independent experiments with each construct. Data are means ±SEM for 0.1 and 50 mM K+with means from individual experiments indicated by the smaller grey symbols. Note the logarithmic scale. Significance at P<0.02 is indicated by lettering. 14051746-1 Figure 4. Non-interacting GORK channel mutations express functional K+ channels with displaced midpoint voltages Representative current traces and steady-state current-voltage (IV) curves recorded under voltage clamp from guard cells of wild-type Arabidopsis (a) and guard cells of the gork mutant background complemented with GFP fusions of wild-type GORK (GORKwt, b), the non-interacting mutations GORKkN-gS1-L4(c) and GORKNP(d), and the interacting GORKPNNPmutation (e) under control of the guard cell pGC1 promoter. IV curves are means ±SE of n>6 independent experiments, each recording comprising measurements from individual guard cells superfused successively with 1 (filled circles), 10 (grey circles), and 30 mM (open circles) K+ outside, cross-referenced by symbol. Scale bar: horizontal, 1 s; vertical, 100 µA cm-2. Lines are joint, least-squares fittings to Eqn [1]. Fittings yielded a common δ of 1.82±0.04. Means ±SE for V1 / 2 from these fittings, summarized in (f), show a significant negative shift for each of the non-interacting mutant channels. Significant differences at P<0.05 across all K+ concentrations are indicated (letters, right). Figure 5. Non-interacting GORK channel mutations accelerate stomatal closure and enhance water use efficiency (a) Stomatal conductance (gs) responses to a 100 min light step of 200 m mol m-2s-1 PAR following a 1-h dark period (above). Simulation outputs (left) are for wild-type (wt), GORK with a -30 mV displacement in V1 / 2 (mGORK; see Fig.4) and for the gork nul mutant. Means ±SE of n>5 independent experiments on wild-type (wt), the nul mutant background (gork), and the same background expressing the GORKNPmutation. (b) Closing rate constants for the simulations (diamonds) and experimental measurements including those in (a). Rate constants were determined from fittings to a first order exponential function and are shown for each measurement (grey circles) and as means ±SE of these data (black circles). Significant differences are indicated (letters, below). (c) Opening halftimes for the simulations (diamonds) and experimental measurements including those in (a). Halftimes are shown for each measurement (grey circles) and as means ±SE of these data (black circles). Significant differences are indicated (letters, below). (d) Representative wild-type, gork mutant and GORKwt, GORKkN-gS1-L4, GORKNPand GORKPNNPcomplemented gork mutant plants after 5 wk growth under fixed and varying light regimes (see Methods). (e,f) Rosette areas (e), dry biomass and water use 14051746-1 efficiencies (f) for all plants, including the plants shown in (d). Small circles are individual plants (open, fixed light; filled, varying light); large circles (open, fixed light; filled, varying light) are means ±SE for each set of plants (wild-type n=11 plants; mutant and complemented n>8 plants). Note the separate WUE scales for plants grown under fixed and varying light. Significant differences are indicated (letters, below). Figure 6. A mechanism coupling GORK clustering and gating through a binding exchange of the VSD N-terminus We start with the assumption that elevating K+ outside facilitates transition from the open channel to a 'locked closed' state, similar to the SKOR K+ channel (left: grey arrow = reduced, black arrow = enhanced bias). As shown, this closed state associates with a shift from binding of the VSD N-terminus (red) with neighbouring channels and clustering (above) at low K+ to internal binding that supports the 'locked closed' state and sensitizes channel gating to K+ (below). Mutating the VSD N-terminus yields a channel (mGORK) impaired in both clustering and internal binding, the latter suppressing the 'locked closed' state K+ inhibition of gating. The mGORK channel thus retains gating characteristics that are closer to the channel clusters, but with a reduced sensitivity to gating inhibition by K+, that enhances K+ flux and hence stomatal kinetics. Figure 7: Truncating the GORK voltage sensor domain beyond the first 23 residues of the N-terminus suppresses interactions with the full-length channel. Figure 8 shows that deleting the first 12 amino acid residues within the N-terminus of GORK achieves a similar or greater effect on channel gating compared to deletion of the first 23 or 50 residues. Effect of N-terminal deletion mutations A) current; B) and C) V1 / 2. Figure 9 shows that single point mutations within the first portion of residues of the N- terminus of GORK produces a significant changes in maximum ensemble conductance (A), the ensemble current (B), and (C) channel gating (measured as the conductance midpoint voltage, V1 / 2). Point substitutions to an alanine residue at positions 3, 5, 6 and 7 of the GORK N-terminus show the most significant change. Figure 10 shows that the effect of single point mutations within the N-terminus are not additive. (A) shows the midpoint voltages for the most effective single mutations in the 14051746-1 N-terminus; (B) shows the current-voltage relations of several single, double and triple mutations within this region of the N-terminus and (C) shows the corresponding midpoint voltages. (D) shows the expression of each of the above constructs as a control. Figure 11 illustrates our working theory of the interactions between the N-terminus and C-terminus of K+ channels. A) GORK channels assemble as tetramers that bring alpha- helices S5 and S6 together around a central pore. B) Trans binding in low K+ concentration between adjacent channels supports channel clustering and depends on binding between charged zipper domains within the N-terminal domain. The N-terminus (ball) and C-linker (hairpin) mediate K+ gating inhibition but not clustering. High K+ leads to loss of trans binding and facilitates cis binding between the N-terminal ball and the C- linker. C) Alignments of GORK, B. oleracea and tomato homologues N-terminus and C- linker domains with examples of conserved residues highlighted. Figure 12 shows enhanced K+ efflux and new K+ influx capacities over the physiological voltage range introduced by suppressing K+ gating inhibition. (A, B) Model current- voltage (IV) curves (A) and K+ flux (B) for the wild-type (wt, black line) and mutant GORK channel with K+ gating inhibition (V1 / 2) displaced by -30 mV (mGORK). IV curve for the KAT current (dashed line, A) included for reference. Inset: IV curves plotted on an expanded current scale. Flux (B) over time with a light step from 10 to 200 µmol m- 2s-1 PAR). (C) IV data from oocytes expressing GORKwt, the GORKkNgS1-L4 zipper domain mutant, GORKDN lacking the first 23 N-terminal residues, and the GORKE317AD321A C-linker mutant. Shading marks substantially enhanced K+ flux capacities. IVs (C, curves) fitted to a Boltzmann function show -35 to -48 mV shifts in V1 / 2 relative to GORK wt (D; lettering, significant differences P<0.02). Figure 13 shows that single residue substitutions within the C-linker domain greatly alter GORK voltage-dependent gating properties and channel activation and deactivation kinetics. E317A and D321A substitution mutations shown. Figure 14 shows that shows that single residue substitutions within the C-linker domain significantly alter GORK A) ensemble current of a voltage-sensitive ion channel, B) voltage-dependent gating properties and C) deactivation kinetics 14051746-1 Figure 15 shows that the effects of single residue mutations within the C-linker domain of GORK exert an additive effect. Figure 16 shows that the effects of single residue mutations within the C-linker domain of GORK exert a significant additive effect. (B, lettering, significant differences P<0.02) Figure 17 confirms the role of negatively charged side chains within the C-linker. E317Q and D321N mutations, i.e. a substitution of negatively charged amino acids for neutral amino acids greatly alters GORK voltage-dependent gating properties and channel activation and deactivation kinetics. Figure 18 confirms the role of negatively charged side chains within the C-linker. E317Q and D321N mutations, i.e. a substitution of negatively charged amino acids for neutral amino acids greatly alters GORK voltage-dependent gating properties and channel activation and deactivation kinetics. (B, significant differences P<0.02). Figure 19 shows that protein structure modelling (SWISS-MODEL) predicts inter-subunit electrostatic coupling with E317 and D321. A salt bridge interaction between E317 or D321 is predicted with K312 of S6 is predicted. Despite four identical subunits, two sets of distinct interactions are predicted. (B, lettering, significant differences P<0.02) Figure 20 shows that the predicted alternating pattern of interactions is supported by voltage clamp data. Figure 21 shows the alignment of voltage-gated potassium channel sequences between Arabidopsis, Glycine Max and Zea Mays. The residues highlighted between residues 1 and 120 of G.max and Z.mays, and residues 1 to 26 of Arabidopsis are conserved residues / motifs and are targets of the technologies presented in this invention herein. The residues comprising the four major alpha helices of the C-linker domain are indicated. The red box indicates the exemplar positions which effect voltage-gating and conductance, i.e. the corresponding positions to 317, 319 to 321, 322 to 326, 330 to 335 and 346. Figure 22 shows that plants with a mutation in the N-terminal domain and the C-linker domain (referred to as the “WeToo” or “Omni-GORK-1” mutant) alters the gating and 14051746-1 slowing of closing kinetics of voltage gated potassium channels to a greater extent than in plants with a mutation in the N-terminal domain (only) or the C-linker domain (only). Plants were Arabidopsis; N-terminal domain mutants had a deletion of the residues 2-23 of the N-terminal; C-linker domain mutants contained a D321A mutation; “We-too” mutants contained both the N-termianld oamin and C-linker domain mutations. Figure 23 shows that mutations in the C-linker domain effect channels kinetics across GORK and SKOR channels. A mutation in GORK (E317A) was translated to the corresponding position in SKOR by a sequence alignment (E334A). The corresponding SKOR mutant revealed that mutations in the C-linker domain in SKOR achieve an even greater significant change in channel-gating kinetics than was observed in GORK. Therefore, corresponding mutations in SKOR, in addition to GORK can be used to alter stomatal kinetics to improve carbon assimilation and water use efficiency in plants. Figure 24 shows that a combination of two mutations in the C-linker of SKOR (E334A:D338A) prevent closing of the SKOR channel entirely, leading to a massive potassium leak and a surprising effect on stomatal kinetics. Figure 25 shows that a combination of mutations in the N-terminal domain and the C- linker domain (A, C, D, E) or in the N-terminal domain and in the S2 domain (B, F, G, H) shows an additive or synergistic effect on channel kinetics compared to single mutations in any domain. Delta 2-23 is a deletion of residues 2-23 of SEQ ID NO: 1 and is a deletion in the N-terminal domain; D321A is a C-linker mutation; mutS2 is an F108S mutation in the S2 domain, specifically position 108 of SEQ ID NO: 1; OmniGORK1 is a combination mutant comprising the D321 and delta 2-23 mutations; OMNIGORK2 is a combination mutation comprising the F108S mutation and delta 2-23 mutations. DETAILED DESCRIPTION OF THE INVENTION The present invention will now be further described. In the following passages, different aspects of the invention are defined in more detail. Each aspect so defined may be combined with any other aspect or aspects unless clearly indicated to the contrary. In particular, any feature indicated as being preferred or advantageous may be combined with any other feature or features indicated as being preferred or advantageous. 14051746-1 The practice of the present invention will employ, unless otherwise indicated, conventional techniques of plant biology, microbiology, tissue culture, molecular biology, chemistry, biochemistry and recombinant DNA technology, bioinformatics which are within the skill of the art. Such techniques are explained fully in the literature. As used herein, the words "nucleic acid", "nucleic acid sequence", "nucleotide", "nucleic acid molecule" or "polynucleotide" are intended to include DNA molecules (e.g., cDNA or genomic DNA), RNA molecules (e.g., mRNA), natural occurring, mutated, synthetic DNA or RNA molecules, and analogs of the DNA or RNA generated using nucleotide analogs. It can be single-stranded or double-stranded. Such nucleic acids or polynucleotides include, but are not limited to, coding sequences of structural genes, anti-sense sequences, and non-coding regulatory sequences that do not encode mRNAs or protein products. These terms also encompass a gene. The term "gene" or “gene sequence” is used broadly to refer to a DNA nucleic acid associated with a biological function. Thus, genes may include introns and exons as in the genomic sequence, or may comprise only a coding sequence as in cDNAs, and / or may include cDNAs in combination with regulatory sequences. The terms "polypeptide" and "protein" are used interchangeably herein and refer to amino acids in a polymeric form of any length, linked together by peptide bonds. The aspects of the invention involve recombination DNA technology and exclude embodiments that are solely based on generating plants by traditional breeding methods. For the purposes of the invention, a “genetically altered plant” or “mutant plant” is a plant that has been genetically altered compared to the naturally occurring wild type (WT) plant. Voltage-sensitive K+channels – including the outward-rectifying channels GORK and closely-related SKOR as well as the inward-rectifying channel KAT1 – belong to the superfamily of so-called Kv channels that are found across all phyla. These proteins form functional channels as tetramers, each protein subunit comprising six transmembrane α- helices with cytosolic N- and C-termini (as shown in Fig. 1A). The first four α-helices (S1-S4) of the subunit form a semi- autonomous voltage-sensor domain (VSD), a structure that is highly conserved among voltage-gated channels. The last two α-helices 14051746-1 (S5-S6) line a water-filled pore through the membrane within the centre of the tetrameric channel assembly. The pore of P region between S5 and S6 α-helices has a short pore helix with a highly conserved TxGYGD (SEQ ID NO: 75) domain serving as the selective filter for potassium. The pore-lining α-helices connect to the VSD through a cytosolic linker that ensures that conformational changes between the VSD and the pore domains occur in 'lockstep'. These channels open and close, in a process called “gating” in response to membrane voltage, as well as the extracellular potassium concentration. Here we demonstrate that the C-linker domain, a hairpin linker domain found after the S6 α-helix and before the C-terminus, also has an important role in gating. The VSD itself incorporates a network of charges that, with a change in voltage, drive VSD conformation and alter its hydration surface as it moves part-way across the membrane, thereby opening the channel pore. GORK and SKOR assembles clusters at submillimolar K+ that reversibly disassembles when K+ is raised to 10 mM and higher concentrations; additionally, clustering is inhibited by the K+ channel blocker Ba+that enters and lodges in the channel pore, preventing K+ permeation and blocking conformational relaxation to the closed state. Thus, it is believed that clustering is connected to gating and that both are characteristics intrinsic to the GORK and SKOR protein itself. Within the plane of the membrane, the VSDs form an outer ring around the channel pore (as shown in Fig. 1A). We have reasoned that clustering between GORK channels within the membrane entails inter-channel interactions between VSDs. The opening and closing of K+ channels is a primary determinant of guard cell turgidity and, by extension, a key determinant of stomatal opening and closing. The following embodiments apply to all aspects of the invention. In one embodiment, the stomatal voltage-gated potassium channel is an outward- rectifying potassium efflux channel (also known as a "Koutchannel"). Koutchannels respond to the extracellular K+concentration. Increasing the concentration of extracellular K+suppresses channel opening in a voltage-dependent manner. In contrast, a low concentration of extracellular K+promotes channel opening. In particular, activation of Kout channels is dependent on membrane depolarization, such that the channels open when the membrane potential shifts to more positive voltages, usually higher than the K+equilibrium voltage (Ek). This allows K+release. In other words, Koutchannels open when membrane voltages are higher than Ek so that the driving force on K+is outward. 14051746-1 In one embodiment, the potassium channel is a GORK (Guard cell Outward Rectifying Potassium (K+)) channel. In another embodiment, the potassium channel is a SKOR (Outward rectifying Shaker-type K+) channel. These channels share similar alternations in charge along their N-termini, as shown in Fig.2a. We have also demonstrated that introducing a mutation into the C-linker region of SKOR also disrupts potassium channel gating kinetics. In fact, we have shown a mutation position originally identified in GORK to alter channel can be translated to the equivalent position in SKOR, to achieve an even greater negative shift in V1 / 2 and increased current inwards than was observed in GORK (Figure 23). The E317 position in GORK corresponds to E334 in SKOR, and a mutation at the E334 position in SKOR leads to an even greater delay in closing compared to the E317 in GORK. In a further embodiment, the amino acid sequence of the GORK channel is selected from one of SEQ ID NOs: 1, 3 and 5 or a functional homologue or variant thereof. In a further embodiment, the nucleic acid sequence of the GORK channel is selected from one of SEQ ID NOs: 2, 4 and 6 or a functional variant or homologue thereof. In another embodiment, the amino acid sequence of the SKOR channel is selected from one of SEQ ID NOs 7, 9, 11, 13, 15, 17, 19 and 21 or a functional variant or homologue thereof. In a further embodiment, the nucleic acid sequence of the SKOR channel is selected from one of SEQ ID NOs: 8, 10, 12, 14, 16, 18, 20 or 22 or a functional variant or homologue thereof. In a further embodiment, the sequence of the stomatal voltage-gated potassium channel is selected from one of the below sequences in Table 1. Table 1: stomatal voltage-gated potassium channel sequences from different organisms. NCIB / G Organism- SEQ ID Organism UniProt enBa nk specific NO: databases Arabidopsis thaliana Q94A76 CAC17380.1 AT5G37500 SEQ ID NO:1 Brassica napus (Rape) A0A078H3V4 XP_01365606 SEQ ID 9.1 NO: 3 14051746-1 Tarenaya hassleriana XP_01055388 5.1 Elaeis guineensis (Oil A0A6I9QAA3 XP_01090545 SEQ ID palm) 4.2 NO: 7 Raphanus sativus (Radish) A0A6J0JE53 XP_01843330 SEQ ID 1.1 NO: 5 Capsicum annuum A0A1U8GYE0 (peppers) KAF3658364. 1 Hibiscus syriacus (Rose of A0A6A2ZB50 XP_03901737 Sharon) 6.1 Triticum aestivum (Wheat) A0A3B6RCP3 XP_04444218 0.1 Oryza sativa (Rice) Q653P0 XP_01564441 SEQ ID 9.1 NO: 9 Gynandropsis gynandra - 12581.1 (C4) Zea mays (maize, C4) A0A1D6LW78 PWZ19722.1 SEQ ID NO: 34 AAW82753.1 SEQ ID NO:35 AQK83496.1 SEQ ID NO: 36 Panicum miliaceum (Proso A0A3L6PAE8 RLM54412.1 millet, C4) Sorghum vulgare A0A194YID1 XP_02130523 (Sorghum bicolor, C4) 9.1 Glycine Max (soybean)KAG4383022.SEQ ID 1 NO: 31 KAG4402628. SEQ ID 1 NO: 33 KAG4402629.1 SEQ ID . NO: 32 XP_00354436 SEQ ID 1.1. NO: 17 In one embodiment, the plant, part thereof or plant cell comprises at least one mutation in one of the above sequences. 14051746-1 In a preferred embodiment, the stomatal voltage-gated potassium channel comprises a sequence selected from (UniProtKB / Swiss-Prot) accession number Q94A76.2; (GenBank) KAG4383022.1, KAG4402628.1, KAG4402629.1., PWZ19722.1, AAW82753.1, AQK83496.1, or (NCBI) XP_003544361.1. We have found that GORK clustering depends on binding between the VSDs of neighbouring channels – as shown in Figure 1. It arises through conserved sequences of alternately charged residues that appear to interact in register between the cytosolic N-termini of the VSDs and their complementary binding sites. This pattern of alternately charged amino acids in the cytosolic N-termini is shown in Figure 2, and is conserved amongst different crops. We show that mutations affecting the pattern of alternate charges affects clustering, which in turn influences the K+-dependence of GORK and SKOR gating. The results from these mutations proved counterintuitive; it was anticipated that impairing clustering would suppress gating and displace the steady-state IV relations to the right along the voltage axis. Yet, paradoxically, mutations suppressing VSD interaction and clustering actually enhanced channel activity as if the channels had nonetheless assembled in clusters. This is shown in Figure 3. In an embodiment, the surprisingly increased channel activity resulting from mutations in the N-termini is a consequence of impaired internal binding, suppressing the ‘locked-closed’ state, leading to enhanced K+flux and stomatal kinetics. We have further found that at the N-terminus there are a number of residues (in particular, at least the first 20 to 30 residues) that in effect act as a “ball”. This “ball” is held away from the pore at low K because the zipper domain (residues~20-60) interact with zipper domains of other channels (the fireman’s grip that leads to clustering). At high K, the zippers separate and allow the N-terminus to fold back so that the ‘ball’ interacts with a C-linker domain just below the pore. In particular, the “ball” may interact with negatively charged residues in the C-linker loop at the base of the channel pore – specifically, we believe that the “ball” may insert into a groove of the C-linker domain, causing the C-linker domain to push against the S4-S5 loops to favour channel closure. The zipper may also help to stabilise this interaction by holding the N-terminus close to the inner surface of the membrane. 14051746-1 As such, we have found that binding and clustering associate with, and impacts on the voltage- and K+-dependencies of GORK channel gating (Figure.4). Most importantly, we show that this feature can be harnessed to accelerate stomatal kinetics and improve WUE without a cost in carbon assimilation. Modelling predicted and experiments demonstrated that manipulating GORK gating to enhance guard cell K+flux accelerated stomatal kinetics as well as promoting stomatal conductance, gs (Figure. 5). These findings present a strategy, based on an ion channel native to the guard cell, for improving stomatal responsiveness and water use by the plant. We also report here, for the first time, that the C-linker, as well as the cytosolic N- terminus, plays a vital role in gating and channel conductance of voltage-gated potassium channels. In a first aspect of the invention there is provided a genetically altered plant, part thereof or plant cell wherein the plant, part thereof or plant cell is characterised by at least one mutation in a stomatal voltage-gated potassium channel, for example, as described above. The genetically altered plant, part thereof or plant cell may comprise at least one mutation in a C-linker domain, as described below. Alternatively, the genetically altered plant, part thereof or plant cell may comprise at least one mutation in the cytosolic N termini of the plant, as described below. Alternatively, the genetically altered plant, part thereof or plant cell may comprise at least one mutation in a C-linker domain, as described below, and at least one mutation in the cytosolic N termini of the plant, as described below. N-terminal mutations In one embodiment, the mutation is in the N-terminus of the potassium channel. In one embodiment, the N-terminus comprises the voltage-sensing domain (VSD). By “VSD” is meant the cytosolic N termini, the S1, S2, S3 and S4 transmembrane alpha helices and the cytosolic loops between S1 and S2, between S2 and S3, between S3 and S4 and between S4 and S5. Accordingly, in one embodiment, the one or more mutation are in the VSD. In a particularly preferred embodiment, the mutation is in the cytosolic N termini. Typically the N termini makes up around the first 100 to 150 amino acids of the potassium channel. 14051746-1 Preferably, the at least one mutation is in the N-terminal 70 (i.e. positions 1-70 or 2-70) amino acids of the potassium channel, more preferably within the N-terminal 60 (i.e. positions 1 to 60 or 2 to 60) amino acids of the potassium channel. In a further preferred embodiment, the mutation is at one or more of positions 20-60, more preferably at one or more of residues at positions 24-59 of the potassium channel. In one embodiment, the mutation is a mutation in the S2 transmembrane alpha helix of a stomatal voltage-gated potassium channel, or in the cytosolic loop between S1 and S2 or in the cytosolic loop between S2 and S3 of a stomatal voltage-gated potassium channel. The Applicant has found that a mutation at positon 108 of SEQ ID NO: 1 – in the S2 region of GORK, a canonical stomatal voltage-gated potassium channel, alters the channel kinetics, reducing the half maximal activation potential (V1 / 2), reducing the activation time and increases the deactivation time compared to a wildtype channel. This is shown in Figure 25 B, F, G and H. Accordingly, in one embodiment, the mutation is a mutation at position 108 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the F residue at position 108, more preferably a F for a negatively charged or neutral amino acid, more preferably a F for a neutral amino acid, such as A, G or L or S. In one embodiment, the mutation is F>S at position 108 of SEQ ID NO: 1. Position 108 of SEQ ID NO: 1 (GORK) corresponds to position 125 of SEQ ID NO: 11 (SKOR). The corresponding F residue can be identified by identifying a QIAFLVD motif in an amino acid sequence of a channel, wherein the F corresponds to the residue. Accordingly, in one embodiment the mutation is a mutation at position 125 of SEQ ID NO: 11 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the F residue at position 125, more preferably a F for a negatively charged or neutral amino acid, more preferably a F for a neutral amino acid, such as A, G or L or S. In one embodiment, the mutation is F>S at position 125 of SEQ ID NO: 11. In one embodiment, the mutation is within the first 30 amino acids of the N-terminus – i.e. at one or more of positions 1 to 30 or 2 to 30. More preferably, the mutation is within the first 20 amino acids of the N-terminus – i.e. at one or more of positions 1 to 20 or 2 14051746-1 to 21. In a further embodiment, the mutation is in the first 10 (i.e. residues 2 to 10) or first 7 residues (i.e. residues 2 to 7) of the potassium channel. In one embodiment, the sequence of the cytosolic N termini comprises SEQ ID NO: 55 or a functional variant or homologue thereof. DDVSSRRGKLSLAETFRWLDSSEHRRIETDGHNDYKYIIHPKNRWYK (SEQ ID NO: 55) In another embodiment, the sequence of the cytosolic N termini comprises one of the following sequences or a functional variant or homologue thereof. 55 63 64 65 66 67 68 Accordingly, in one embodiment, the plant, part thereof or plant cell comprises at least 69 70 one mutation in the cytosolic N termini of the channel, wherein the mutation prevents 71 72 clustering of the channel. As shown in Figure 1, the skilled person could, as an example, 73 use the mating-based split ubiquitin screen (mbSUS), to determine whether a candidate 74 mutation affects (i.e. prevents or reduces) clustering of the channel. As used herein, by “clustering” is meant the process by which individual potassium channels (each of which are made up of four subunits to form a tetramer) assemble or cluster together as a result of interactions between the VSDs at the periphery of the tetramer (Fig.1a (1) and (2)). In a further embodiment, the plant, part thereof or plant cell comprises at least one mutation in the cytosolic N termini whereby the mutation alters the pattern of charged amino acids in the cytosolic N termini. In one embodiment, “altering the pattern” means that where the cytosolic N termini comprises an alternating pattern of charged residues – that is, one or more positively charged residues followed by one or more negatively charged residues, or vice versa, with or without neutral amino acids interspersed in- between, followed by one or more positively charged residues and so on – this alternating pattern of residues is altered or changed by mutation such that the alternating pattern in part or in full is disrupted. For example – in a pattern of positive-negative- positive-negative-positive residues, as shown in Figure 2, one or more of the charged residues / regions may be mutated to positive or negative residues. 14051746-1 As shown in Figure 2, the wild-type cytosolic N termini of GORK comprises an alternating pattern of positive and negative amino acids. Mutation of the charged (positive) residues to negative residues (Figure 2b and c – gVSDPN) or mutation of the charged (negative) residues to positive residues (Figure 2b and c – gVSDNP) prevents clustering of the potassium channel. Accordingly, in one embodiment, the plant, part thereof or plant cell comprises at least one mutation in the cytosolic N termini of the channel, wherein the mutation is the substitution of one or more negatively charged residues for positively charged residues or neutral residues. Preferably, enough residues are substituted to change the pattern of charged residues in the sequence. More preferably, all negatively charged residues are substituted for positively charged residues or neutral residues. In another embodiment, the plant, part thereof or plant cell comprises at least one mutation in the cytosolic N termini of the channel, wherein the mutation is the substitution of one or more positively charged residues for negatively charged residues or neutral residues. Preferably, enough residues are substituted to change the pattern of charged residues in the sequence. More preferably, all negatively charged residues are substituted for positively charged residues or neutral residues. Positively charged amino acids are Lysine (K), Arginine (R) and Histidine (H). Negatively charged amino acids are: Aspartic Acid (D) and Glutamic acid (E). Neutral amino acids are: Glycine (G), Alanine (A), Valine (V), Cysteine (C), Proline (P), Leucine (L), Isoleucine (I), Methionine (M), Tryptophan (W), Phenylalanine (F), Serine (S), Threonine (T), Tyrosine (Y), Asparagine (N) and Glutamine (Q). However, as shown in Figure 3, reversing the alternating pattern of charged residues (gVSDPNNP) had no effect on clustering. Accordingly, the invention does not comprise a plant, part thereof or plant cell where the pattern of charged amino acid residues in the cytosolic N termini has been reversed. In one embodiment, therefore, the plant does not comprise a mutation in the cytosolic N termini where the mutation is the substitution of 14051746-1 all positively charged residues for negatively charged residues and the substitution of all negatively charged residues for positively charged residues. In a further embodiment, the plant, part thereof or plant cell, may contain at least one mutation in the cytosolic N termini and further, at least one mutations in the S1, S2, and / or S3 loop and / or the S4 / S5 linker. In another embodiment, the mutation is a deletion of one or more amino acids in the cytosolic N termini. Preferably, the mutation is the deletion of all amino acids in the cytosolic N termini. In one embodiment, the mutation is the deletion of the first 60 residues (i.e. residues 2 to 59). Alternatively, the mutation is the deletion of the first 30 residues (i.e. residues 2 to 30), or the deletion of the first 23 residues (i.e. residues 2 to 23) or the deletion of the first 12 residues (i.e. residues 2 to 12). In another embodiment, the mutation is the deletion of the first 10 residues (i.e. residues 2 to 10). In another embodiment, the mutation is the deletion of the first 7 residues (i.e. residues 2 to 7). In particular, as shown in Figure 8, we have found that deletion of residues 2 to 12 of the cytosolic N-terminus achieves the same or a greater effect than a deletion of a larger scale of residues, i.e. residue 2 to 50 and 2 to 23 respectively. In particular, we observed that the change in V1 / 2 is even greater when residues 2 to 12 of the N-terminus are deleted compared to residues 2 to 50 (although a significant change is observed for both). We have also identified that single mutations of key residues within the N-terminus has a significant effect on channel gating and conductance. As shown in Figure 9, single residue substitutions at positions 3, 5, 6 and 7 of SEQ ID NO: 1 achieve impressive changes in conductance, current and V1 / 2. Figure 10 shows that mutations at single residues within the N-terminus do not have an additive effect, and so a single mutation is sufficient to achieve this effect. Accordingly, in one embodiment, the mutation is a substitution of at least one amino acid within the first 20 residues, preferably within the first 10 residues, and even more preferably within the first 7 residues of the N-terminus of the potassium channel. 14051746-1 In a preferred embodiment, the mutation is a substitution of at least one positively charged residue for a neutral or negatively charged residue. Alternatively, the mutation is the substitution of at least one negatively charged residue for a positively charged or neutral residue. In one embodiment, the mutation is a mutation of an arginine (R) residue at least one position selected from 3, 5, 6 and 7 of SEQ ID NO: 1 of the N-terminus of GORK channel, or an equivalent position of a functional homologue or variant thereof. In an even more preferred embodiment, the substitution mutation is a substitution of an arginine, for a neutral residue, such as alanine. As shown in Figure 10, the above mutation of arginine residues caused a left-shift in gating (approx. -30 to -40mV) in Arabidopsis, (a left-shift is the same as increasing the activity of the channel). C-linker domain mutations We have also identified that mutations at single amino acid residues within a C-linker domain of the potassium channel produce significant changes in the stomatal voltage- gated potassium channel kinetics. The scale of the change resulting from individual residue mutations was unexpected. As shown in Figures 13 and 14, mutating only a single residue within this C-linker domain is sufficient to achieve a significant change in channel sensitivity (V1 / 2) and channel current in GORK compared to the wild-type channel. Accordingly, in another embodiment, the at least one mutation is in the C-linker domain of the potassium channel. By “C-linker domain” it is meant the hairpin after the S6 α-helix and before the C- terminus. The C-linker domain may be considered a distinct structure to the S6 α-helix and C-terminus. The C-linker domain is characterised by four α-helices, namely A’, B’, C’ and D’ α-helices. In one embodiment, the sequence of the C-linker domain comprises positions 312 to 387 of SEQ ID NO: 1 or corresponding positions in a homologous sequence. Accordingly, in one embodiment, there is at least one mutation between positions 312 and 387 of SEQ ID NO: 1 or corresponding positions in a homologous sequence, wherein the mutation is 14051746-1 not at position 313 of SEQ ID NO: 1. In one embodiment, the homologous sequence may comprise a sequence selected from SEQ ID NO: 56 to 62 or a functional variant or homologue thereof. For all aspects and embodiments of the invention, the scope of this invention does not include a mutation at position 313 of SEQ ID NO: 1, and specifically not to a substitution of a glycine residue at position 313 of SEQ ID NO: 1. The at least one mutation may be in at least one of the A’ or B’ or C’ or D’ α-helices. In one embodiment, a mutation may also or alternatively be within the residues between two α-helices. In one embodiment, the mutation is in the A’ α-helix of the C-linker domain, and is not a mutation at position 313 of SEQ ID NO: 1. The A’ α-helix of the C-linker domain may comprise a sequence selected from SEQ ID NO: 37 to 39. The B’ α-helix of the C-linker domain may comprise a sequence selected from SEQ ID NO: 40 to 42. The C’ α-helix of the C-linker domain may comprise a sequence selected from SEQ ID NO: 43 to 45. The D’ α-helix of the C-linker domain may comprise a sequence selected from SEQ ID NO: 46 to 48. The C-linker domain of K+channels also characteristically contain a highly conserved (K / R)LGR domain, as shown in the sequence alignments of Figure 21. This conserved domain spans the C’ terminal of the A’ domain and the N terminal of the B’ domain and the residues in-between. Given the high conservation of this domain, and the importance of neighbouring residues within gating, it is highly likely that the conserved (K / R)LGR domain is an important determinant of K+ channel sensitivity. Accordingly, in an alternative embodiment, the at least one mutation is in the (K / R)LGR domain of the C- linker domain of a voltage-gated potassium channel. Other conserved motifs within the C-linker domain include: 14051746-1 - a EKFRD motif within the A’ helix - a RLQY(D / E) motif within the B’ helix. Accordingly, in one embodiment, the at least one mutation is in the (K / R)LGR, EKRRD and / or RLQY(D / E) domain of the C-linker of a voltage-gated potassium channel. The conservation of these motifs between voltage-gated potassium channels in Arabidopsis, Glycine Max and Zea Mays are highlighted in Figure 21. We believe that the N-terminus is interacting with the C-linker domain via the conserved residues and motifs within the first portion of residues of the N-terminus. It is our understanding that the first portion of the N-terminus acts like a ball that binds to charged residues and / or motifs within the C-linker to affect clustering and / or gating (as illustrated in Figure 11B). The residues anticipated to be involved in this interaction are highlighted in Figure 11C. The mutation may be a substitution of one amino acid for another amino acid or a deletion or addition of one or more amino acids. Preferably, the mutation is a substitution mutation. Alternatively, the mutation is a deletion. In one embodiment, the mutation is the deletion of the entire C-linker domain, for example, as described above. In another embodiment, the mutation is the deletion of one or more of the A’ α-helix, the B’ α-helix the C’ α-helix and / or the D’ α-helix. In particular, we have identified that the greatest changes in K+channel voltage- dependent gating properties and channel activation / deactivation kinetics are observed when negatively-charged amino acids in the C-linker domain are mutated to an amino acid of a different charge. This is shown in Figures 17 and 18; substitution of the E317 and D321 residues to a neutrally charged amino acid (Q and N, respectively) significantly alters channel voltage-gating and deactivation. The scale of the change was completely unexpected. Figure 18C shows the deactivation half-time of the mutated channels increases from ~30ms to ~2000 ms (E317Q) and ~2500 ms (D321N), i.e. a 66-fold and 83-fold increase respectively. 14051746-1 Accordingly, in one embodiment, the genetically altered plant, part thereof or plant cell comprises at least one mutation in the C-linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is the substitution of one or more negatively charged residues for one or more positively charged residues or one or more neutral residues or the substitution of one or more positively charged residues for one or more negatively charged or one or more neutral residues or one or more residues with a larger mass. Preferably, enough residues are substituted to disrupt the interaction of the C- linker and the N-terminus of the channel described above. More preferably, all negatively charged residues are substituted for positively charged residues or neutral residues or vice versa. Even more preferably, the mutation is a substitution of an amino acid to an alanine or arginine or glutamine residue. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 312 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 312, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K312A at position 312 of SEQ ID NO: 1; - A mutation at position 316 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 316, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 317 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 317, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E317A at position 317 of SEQ ID NO: 1; - A mutation at position 318 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 318, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 319 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F 14051746-1 residue at position 319, more preferably a F for a negatively charged or positively charged amino acid, - A mutation at position 320 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 320, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 321 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 321, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D321A at position 321 of SEQ ID NO: 1; - A mutation at position 332 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 332, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 333 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K or N residue at position 333, more preferably a K or N for a negatively charged or positively charged amino acid or neutral amino acid; - A mutation at position 334 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K or R residue at position 334, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; - A mutation at position 335 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 335, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 336 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 336, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 337 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R 14051746-1 residue at position 337, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 348 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 348, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 349 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 349, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 350 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 350, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 351 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 351, more preferably a Y for a negatively charged or positively charged amino acid; - A mutation at position 352 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 352, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L; - A mutation at position 356 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a T residue at position 356, more preferably a T for a negatively charged or neutral amino acid, more preferably a T for a neutral amino acid, such as A, G or L; and wherein the mutation is not a substitution mutation at position 313 of SEQ ID NO: 1. We have also identified positions in SKOR channels that can be used to achieve altered channel kinetics. In Figure 23, we have shown that a mutation at position E334 of SKOR, corresponding to E317 in GORK, also alters channel kinetics by increasing the negative shift in V1 / 2 and delaying the closing of the channel. 14051746-1 Accordingly, in one embodiment, the mutation is at position 334 of SEQ ID NO: 11, or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 334, more preferably a E for a charged amino acid such as A, G or L, most preferably E334A. We have shown in Figures 23 and 24 that a mutation at this position drastically disrupts channel kinetics compared to the wild type. We have also identified the corresponding position of position 334 in SED ID NO: 11 in a range of homologous sequences found in crop plants. Accordingly, in one embodiment, the mutation is selected from: ^ position 335 of SEQ ID NO: 13, ^ position 336 of SEQ ID NO: 15 ^ position 358 of SEQ ID NO: 17 ^ position 400 of SEQ ID NO: 31 ^ position 357 of SEQ ID NO: 32 or 33 ^ position 334 of SEQ ID NO: 34 ^ position 269 of SEQ ID NO: 35 ^ position 334 of SEQ ID NO: 36 ^ position 7 of SEQ ID NO: 38 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue for a neutral amino acid residue such as A, G or L, most preferably a E>A substitution. We have found that positions in GORK that can be mutated to alter channel kinetics can be translated into SKOR by identifying the corresponding position. It is possible to identify a corresponding position in a homologous sequence by sequence alignment. Specifically, in respect of the 317 and 321 positions identified in GORK, they can be identified in SKOR or an alternative voltage-gated channel by identifying the sequence ‘E(K / R)F(R / Y)D’, wherein the E and D correspond to positons 334 and 338 of SKOR Figure 24. The position D321 in SEQ ID NO: 1, i.e., GORK corresponds to position 338 of SEQ ID NO: 11 i.e., SKOR in the same species. Accordingly, in one embodiment, the mutation is at position 338 of SEQ ID NO: 11 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 14051746-1 338, more preferably a D for a neutral amino acid residue such as A, G or L, most preferably a E>A substitution. We have also identified the corresponding position of position 338 in SED ID NO: 11 in a range of homologous sequences found in crop plants. Accordingly, in one embodiment, the mutation is selected from: ^ position 339 of SEQ ID NO: 13; ^ position 340 of SEQ ID NO: 15; ^ position 362 of SEQ ID NO: 17; ^ position 335 of SEQ ID NO: 19; ^ position 335 of SEQ ID NO: 21; ^ position 403 of SEQ ID NO: 31; ^ position 361 of SEQ ID NO: 32 or 33; ^ position 338 of SEQ ID NO: 34; ^ position 273 of SEQ ID NO: 35; ^ position 338 of SEQ ID NO: 36; ^ position 7 of SEQ ID NO: 11; or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue for a neutral amino acid residue such as A, G or L, most preferably a E>A substitution. Surprisingly our data has shown that mutations of more than one residue within the C- linker in GORK has an additive effect, i.e. the effects observed increases with each mutation. This is shown in Figures 15 and 16, where the channel deactivation kinetics of the double-mutant of E317A:D321A is significantly greater than that observed for E317A or D321A alone. In particular, the deactivation time of the channel is greatly delayed by mutations within the C-linker; see Figure 15 and figure 16C. This delay in channel deactivation results in faster opening / closing of the stomata. Figure 12 also highlights the significant change in channel kinetics following mutation of the C-linker or the N-terminus. Surprisingly, mutating two residues within the C-linker produced an even greater change in channel kinetics than mutations in the N-terminus, and greater again than a deletion of the N-terminus cytosolic region. 14051746-1 In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E317 and D321 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312 and E317 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312 and D321 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312, E317 and D321 of SEQ ID NO:1. In one embodiment, the mutation may not be a substitution mutation at position 313 of SEQ ID NO: 1. In one embodiment, the mutation is in a Glycine Max voltage-gated potassium channel. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 395 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 395, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K395A at position 395 of SEQ ID NO: 31; - A mutation at position 399 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 399, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 400 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 400, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E400A at position 400 of SEQ ID NO: 31; - A mutation at position 401 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 401, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K401A at position 401 of SEQ ID NO: 31; - A mutation at position 402 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 402, more preferably a F for a negatively charged or positively charged amino acid, 14051746-1 - A mutation at position 403 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 403, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 404 SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 404, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D404A at position 404 of SEQ ID NO: 31; - A mutation at position 415 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 415, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 416 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 332, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; - A mutation at position 417 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 417, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; - A mutation at position 418 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 418, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 419 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 419, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 420 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 420, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 431 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R 14051746-1 residue at position 431, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 432 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 432, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 433 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 433, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 434 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 434, more preferably a Y for a negatively charged or positively charged amino acid; - A mutation at position 435 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 435, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E400 and D404 of SEQ ID NO: 31. In another embodiment, the mutation is a mutation of K395 and E400 of SEQ ID NO: 31. In another embodiment, the mutation is a mutation of K395 and D404 of SEQ ID NO: 31. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K395, E400 and D404 of SEQ ID NO: 31. In one embodiment, the mutation may not be a substitution mutation at position 396 of SEQ ID NO: 31. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 352 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 352, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K352A at position 352 of SEQ ID NO: 32; 14051746-1 - A mutation at position 356 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 356, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 357 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 357, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E357A at position 357 of SEQ ID NO: 33. - A mutation at position 358 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 358, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K358A at position 358 of SEQ ID NO: 32; - A mutation at position 359 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 359, more preferably a F for a negatively charged or positively charged amino acid, - A mutation at position 360 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 360, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 361 SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 361, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D361A at position 361 of SEQ ID NO: 32; - A mutation at position 372 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 372, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 373 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 373, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; 14051746-1 - A mutation at position 374 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 374, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; - A mutation at position 375 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 375, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 376 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 376, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 377 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 377, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 388 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 388, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 389 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 389, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 390 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 390, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 391 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 391, more preferably a Y for a negatively charged or positively charged amino acid; - A mutation at position 392 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E 14051746-1 residue at position 392, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E357 and D361 of SEQ ID NO: 32. In another embodiment, the mutation is a mutation of K352 and E357 of SEQ ID NO: 32. In another embodiment, the mutation is a mutation of K352 and D361 of SEQ ID NO: 32. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K352, E357 and D361 of SEQ ID NO: 32. In one embodiment, the mutation may not be a substitution mutation at position 353 of SEQ ID NO: 32. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 352 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 352, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K352A at position 352 of SEQ ID NO: 33; - A mutation at position 356 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 356, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 357 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 357, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E357A at position 357 of SEQ ID NO: 33. - A mutation at position 358 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 358, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K358A at position 358 of SEQ ID NO: 33; - A mutation at position 359 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F 14051746-1 residue at position 359, more preferably a F for a negatively charged or positively charged amino acid, - A mutation at position 360 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 360, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 361 SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 361, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D361A at position 361 of SEQ ID NO: 33; - A mutation at position 372 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 372, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 373 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 373, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; - A mutation at position 374 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 374, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; - A mutation at position 375 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 375, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 376 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 376, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 377 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 377, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; 14051746-1 - A mutation at position 388 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 388, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 389 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 389, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 390 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 390, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 391 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 391, more preferably a Y for a negatively charged or positively charged amino acid; - A mutation at position 392 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 392, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E357 and D361 of SEQ ID NO: 33. In another embodiment, the mutation is a mutation of K352 and E357 of SEQ ID NO: 33. In another embodiment, the mutation is a mutation of K352 and D361 of SEQ ID NO: 33. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K352, E357 and D361 of SEQ ID NO: 33. In one embodiment, the mutation may not be a substitution mutation at position 353 of SEQ ID NO: 33. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 353 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 353, more preferably a K for a negatively charged or neutral 14051746-1 amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K354A at position 354 of SEQ ID NO: 17; - A mutation at position 357 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 357, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 358 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 359, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E358A at position 358 of SEQ ID NO: 17; - A mutation at position 359 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 359, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K359A at position 359 of SEQ ID NO: 17; - A mutation at position 360 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 360, more preferably a F for a negatively charged or positively charged amino acid, - A mutation at position 361 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 361, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 362 SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 362, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D362A at position 362 of SEQ ID NO: 17; - A mutation at position 373 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 373, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 374 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N 14051746-1 residue at position 374, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; - A mutation at position 375 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 375, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; - A mutation at position 376 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 376, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 377 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 377, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 378 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 378, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 389 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 389, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 390 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 390, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 391 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 391, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 392 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 392, more preferably a Y for a negatively charged or positively charged amino acid; 14051746-1 - A mutation at position 393 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 393, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. and wherein the mutation is not a substitution mutation at position 354 of SEQ ID NO: 17. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E358 and D362 of SEQ ID NO: 17. In another embodiment, the mutation is a mutation of K353 and E358 of SEQ ID NO: 17. In another embodiment, the mutation is a mutation of K353 and D362 of SEQ ID NO: 17. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K353, E358 and D362 of SEQ ID NO: 17. In one embodiment, the mutation may not be a substitution mutation at position 354 of SEQ ID NO: 17. In one embodiment, the mutation is in a Zea Mays voltage-gated potassium channel. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 329 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 329, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K329A at position 329 of SEQ ID NO: 34 or 36; - A mutation at position 333 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 333, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 334 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 334, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E334A at position 334 of SEQ ID NO: 34 or 36; 14051746-1 - A mutation at position 335 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 335, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is R335A at position 335 of SEQ ID NO: 34 or 36; - A mutation at position 336 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 336, more preferably a F for a negatively charged or positively charged amino acid, - A mutation at position 337 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 337, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 338 SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 338, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D338A at position 338 of SEQ ID NO: 34 or 36; - A mutation at position 349 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 349, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 350 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 350, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; - A mutation at position 351 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 351, more preferably a K for a negatively charged or neutral amino acid, more preferably K for a neutral amino acid, such as A, G or L; - A mutation at position 352 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 352, more preferably a L for a negatively charged or positively charged amino acid; 14051746-1 - A mutation at position 353 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 353, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 354 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 354, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; - A mutation at position 365 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 365, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 366 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 366, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 367 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 367, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 368 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 368, more preferably a Y for a negatively charged or positively charged amino acid; - A mutation at position 369 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 369, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E334 and D338 of SEQ ID NO: 34 or 36. In another embodiment, the mutation is a mutation of K329 and E334 of SEQ ID NO: 34 or 36. In another embodiment, the mutation is a mutation of K329 and D338 of SEQ ID NO: 34 or 36. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. 14051746-1 In one embodiment, the mutation is a mutation of K329, E334 and D338 of SEQ ID NO: 34 or 36. In one embodiment, the mutation may not be a substitution mutation at position 330 of SEQ ID NO: 34 or 36. In one embodiment, the mutation may be selected from one or more of the following mutations: - A mutation at position 264 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 264, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K264A at position 264 of SEQ ID NO: 35; - A mutation at position 268 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 268, more preferably a T for a positively charged or negatively charged amino acid; - A mutation at position 269 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 269, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E269A at position 269 of SEQ ID NO: 35; - A mutation at position 270 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 270, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is R270A at position 270 of SEQ ID NO: 35; - A mutation at position 271 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 271, more preferably a F for a negatively charged or positively charged amino acid, - A mutation at position 272 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 272, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 273 SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D 14051746-1 residue at position 273, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D273A at position 273 of SEQ ID NO: 35; - A mutation at position 284 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 284, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 285 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 285, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; - A mutation at position 286 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 286, more preferably a K for a negatively charged or neutral amino acid, more preferably K for a neutral amino acid, such as A, G or L; - A mutation at position 287 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 287, more preferably a L for a negatively charged or positively charged amino acid; - A mutation at position 288 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 288, more preferably a G for a positively charged or negatively charged amino acid; - A mutation at position 289 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 289, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; - A mutation at position 300 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 300, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; - A mutation at position 301 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 301, more preferably a L for a negatively charged or positively charged amino acid; 14051746-1 - A mutation at position 302 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 302, more preferably a Q for a negatively charged or positively charged amino acid; - A mutation at position 303 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 303, more preferably a Y for a negatively charged or positively charged amino acid; - A mutation at position 304 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 304, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E269 and D273 of SEQ ID NO: 35. In another embodiment, the mutation is a mutation of K264 and E269 of SEQ ID NO: 35. In another embodiment, the mutation is a mutation of K264 and D273 of SEQ ID NO: 35. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K264, E269 and D273 of SEQ ID NO: 35. In one embodiment, the mutation may not be a substitution mutation at position 330 of SEQ ID NO: 35. Our data has also shown that mutations of more than one residue within the C-linker of SKOR channels has an additive effect, i.e. the effects observed increases with each mutation. This is shown in Figure 24 in respect of SKOR where the channel deactivation kinetics of the double-mutant of E334A:D338A is significantly greater than that observed for E334A or D338A alone. In particular, the deactivation time of the channel is greatly delayed by mutations within the C-linker; the double C-linker mutant channel does not close, and permits a large leak current. This failure to close the channel deactivation results in drastic changes in the rate of opening / closing of the stomata. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations described for SKOR. In one embodiment, the mutation is a mutation of E334 and D338 of SEQ ID NO: 11, wherein preferably the mutation is a substitution for 14051746-1 a neutral amino acid, such as A, G or L; most preferably, the mutation is E334A and D338A. In one embodiment, the mutation may comprise at least two mutations selected from: ^ position E335 and D339 of SEQ ID NO: 13, ^ position E336 and D340 of SEQ ID NO: 15 ^ position E358 and D362 of SEQ ID NO: 17 ^ position E400 and D404 of SEQ ID NO: 31 ^ position E357 and D361 of SEQ ID NO: 32 or 33 ^ position E334 and D338 of SEQ ID NO: 34 ^ position E269 and D273 of SEQ ID NO: 35 ^ position E334 and D338 of SEQ ID NO: 36 ^ position E7 and D11 of SEQ ID NO: 38 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution for a neutral amino acid, such as A, G or L; most preferably, the mutation is E>A and D>A. Preferably, the mutation (i.e. any of the above-described mutations) within the C-linker alters the kinetics of the stomatal voltage-gated potassium channel. In one embodiment, the kinetics of the stomatal voltage-gated potassium channel is measured as the sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage-sensitive ion channel (I). In a preferred embodiment, the mutation increases the sensitivity of the gate to a change in voltage (V1 / 2) (resulting in a more negative V1 / 2 value); and / or increases the maximum ensemble conductance (Gmax) and / or increases the ensemble current of a voltage-sensitive ion channel (I). Preferably, the change in channel kinetics is measured relative to a wild-type channel. Without being bound by theory, we believe that mutations of at least one residue within the C-linker may disrupt the interaction with the first 20 residues of the N-terminal domain (i.e., the ball). Loss of this interaction significantly increases both the sensitivity of the channel to K+and the conductance of the channel. This significant change in the stomatal voltage-gated potassium channel kinetics results in accelerated stomatal responses. 14051746-1 Accordingly, in one embodiment, the mutation within the C-linker disrupts the interaction with the N-terminus of a stomatal voltage-gated potassium channel. Preferably, the mutation within the C-linker disrupts the interaction with the cytosolic N termini of a stomatal voltage-gated potassium channel. This may be achieved by introducing a mutation to the C-linker domain only, the N-terminal domain only or both, i.e. a mutation in both the C-linker and the N-terminal domain. Any of the mutations described herein may be selected to achieve mutations in both the C-linker and N-terminal domain. N-terminal and C-linker double mutations Figure 22 shows that plants with a mutation in the N-terminal domain and the C-linker domain (referred to as the “WeToo” mutant or OmniGORK1 mutant) can drastically alter the kinetics of potassium voltage-gated channels. Figures 25 A, C, D and E indicates that such a combination has an additive or even a synergistic effect. Specifically, deleting the first 23 residues of the N-terminal domain and also mutating D321 to Ala results in almost -100 mV shift in gating and slowing of closing kinetics. The data shows an additive effect of the two sites, compared to a mutation in the N-terminal domain only and a mutation in the C-linker domain only. Surprisingly, the double mutant in both the C-linker and N-terminal domain alters deactivation kinetics of potassium voltage-gated channels, to a sigmoid shape. This indicates a drastic change in the conformation of the channel, and implies a synergy between the N-terminus and the C-linker. Accordingly, in one aspect of the invention, there is provided a genetically altered plant, plant part or plant cell, wherein the plant is characterised by at least one mutation in a N-terminal cytosolic domain of a stomatal voltage-gated potassium channel, and further at least one mutation in the C-linker domain of a stomatal voltage-gated potassium channel. According to any other aspect of any method of the invention, the method comprises introducing at least one mutation in a N-terminal cytosolic domain of a stomatal voltage- gated potassium channel, and further at least one mutation in the C-linker domain of a stomatal voltage-gated potassium channel of a plant, plant part thereof or plant cell. In one embodiment, the stomatal voltage-gated potassium channel is GORK. Specific embodiments in respect of GORK channels are described below: 14051746-1 In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is selected from: K312, E317, D321 of SEQ ID NO: 1 or a corresponding position in a homologous sequence. That is, in one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of residues 2-32 or 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at positon 312 of SEQ ID NO: 1, preferably is a substitution of K312 to a neutral amino acid, most preferably is K312A, or a corresponding position in a homologous sequence. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of residues 2-32 or 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at positon 317 of SEQ ID NO: 1, preferably is a substitution of E317 to a neutral amino acid, most preferably is E317A or a corresponding position in a corresponding mutation. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-32 or 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at positon 321 of SEQ ID NO: 1, preferably is a substitution of D321 to a neutral amino acid such as from A, G or L, most preferably is D321A, or a corresponding position in a corresponding mutation. The effect of this combination of mutations is shown in Figures 22 and Figures 25 A and D. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-32 or 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at least two mutations at positions selected from K312, E317, D321 of SEQ ID NO: 1 or at least two corresponding positions in a homologous sequence. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E317 and D321 of 14051746-1 SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312 and E317 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312 and D321 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312, E317 and D321 of SEQ ID NO:1. In all embodiments, the mutation is not a substitution mutation at position 313 of SEQ ID NO: 1. In one embodiment, the mutation is at least two corresponding positions of the C-linker domain mutation positions K312, E317 and D321 of SEQ ID NO: 1 in a homologous sequence are selected from: a. K395, E400 and D404 of SEQ ID NO: 31; or b. K352, E357 and D361 of SEQ ID NO: 32 or 33; or c. K353, E358 and D362 of SEQ ID NO: 17. Alternatively, the at least two corresponding positions of a homologous sequence are selected from: d. K329, E334 and D338 of SEQ ID NO: 34 or 36; or e. K264, E269 and D273 of SEQ ID NO: 35. That is, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2- 23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at least two mutations at positions selected from a. K312, E317, D321 of SEQ ID NO: 1 b. K395, E400 and D404 of SEQ ID NO: 31; or c. K352, E357 and D361 of SEQ ID NO: 32 or 33; or d. K353, E358 and D362 of SEQ ID NO: 17. e. K329, E334 and D338 of SEQ ID NO: 34 or 36; or f. K264, E269 and D273 of SEQ ID NO: 35. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-32, preferably 2-23, of the cytosolic N-terminal (SEQ ID NO: 1) and the mutation in the C-linker domain is two mutations at positions E317 and D321 of SEQ ID NO: 1 or at least two corresponding positions in a homologous sequence, wherein preferably the C-linker domain mutations are E317A and D321A. 14051746-1 In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the further mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 312 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 312, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K312A at position 312 of SEQ ID NO: 1; and / or - A mutation at position 316 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 316, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 317 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 317, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E317A at position 317 of SEQ ID NO: 1; and / or - A mutation at position 318 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 318, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 319 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 319, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 320 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 320, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 321 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D 14051746-1 residue at position 321, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D321A at position 321 of SEQ ID NO: 1; and / or - A mutation at position 332 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 332, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 333 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K or N residue at position 333, more preferably a K or N for a negatively charged or positively charged amino acid or neutral amino acid; and / or - A mutation at position 334 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K or R residue at position 334, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; and / or - A mutation at position 335 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 335, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 336 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 336, more preferably a G for a positively charged or negatively charged amino acid; and / or - A mutation at position 337 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 337, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 348 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 348, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or 14051746-1 - A mutation at position 349 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 349, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 350 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 350, more preferably a Q for a negatively charged or positively charged amino acid; and / or - A mutation at position 351 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 351, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 352 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 352, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L; and / or - A mutation at position 356 of SEQ ID NO: 1 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a T residue at position 356, more preferably a T for a negatively charged or neutral amino acid, more preferably a T for a neutral amino acid, such as A, G or L; and wherein the mutation is not a substitution mutation at position 313 of SEQ ID NO: 1. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the further mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 353 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 353, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K354A at position 354 of SEQ ID NO: 17; and / or - A mutation at position 357 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the 14051746-1 T residue at position 357, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 358 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 359, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E358A at position 358 of SEQ ID NO: 17; and / or - A mutation at position 359 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 359, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K359A at position 359 of SEQ ID NO: 17; and / or - A mutation at position 360 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 360, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 361 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 361, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 362 SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 362, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D362A at position 362 of SEQ ID NO: 17; and / or - A mutation at position 373 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 373, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 374 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 374, more preferably a N for a negatively charged or neutral 14051746-1 amino acid, more preferably a N for a neutral amino acid, such as A, G or L; and / or - A mutation at position 375 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 375, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 376 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 376, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 377 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 377, more preferably a G for a positively charged or negatively charged amino acid; and / or - A mutation at position 378 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 378, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 389 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 389, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 390 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 390, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 391 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 391, more preferably a Q for a negatively charged or positively charged amino acid; and / or - A mutation at position 392 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y 14051746-1 residue at position 392, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 393 of SEQ ID NO: 17 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 393, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L; and wherein the mutation is not a substitution mutation at position 354 of SEQ ID NO: 17. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the further mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 395 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 395, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K395A at position 395 of SEQ ID NO: 31; and / or - A mutation at position 399 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 399, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 400 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 400, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E400A at position 400 of SEQ ID NO: 31; and / or - A mutation at position 401 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 401, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K401A at position 401 of SEQ ID NO: 31; and / or - A mutation at position 402 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F 14051746-1 residue at position 402, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 403 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 403, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 404 SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 404, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D404A at position 404 of SEQ ID NO: 31; and / or - A mutation at position 415 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 415, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 416 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 332, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; and / or - A mutation at position 417 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 417, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 418 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 418, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 419 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 419, more preferably a G for a positively charged or negatively charged amino acid; and / or 14051746-1 - A mutation at position 420 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 420, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 431 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 431, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 432 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 432, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 433 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 433, more preferably a Q for a negatively charged or positively charged amino acid; and / or - A mutation at position 434 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 434, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 435 of SEQ ID NO: 31 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 435, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 352 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 352, more preferably a K for a negatively charged or neutral 14051746-1 amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K352A at position 352 of SEQ ID NO: 32; and / or - A mutation at position 356 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 356, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 357 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 357, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E357A at position 357 of SEQ ID NO: 33; and / or - A mutation at position 358 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 358, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K358A at position 358 of SEQ ID NO: 32; and / or - A mutation at position 359 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 359, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 360 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 360, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 361 SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 361, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D361A at position 361 of SEQ ID NO: 32; and / or - A mutation at position 372 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 372, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or 14051746-1 - A mutation at position 373 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 373, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; and / or - A mutation at position 374 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 374, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 375 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 375, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 376 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 376, more preferably a G for a positively charged or negatively charged amino acid; and / or - A mutation at position 377 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 377, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 388 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 388, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 389 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 389, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 390 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 390, more preferably a Q for a negatively charged or positively charged amino acid; and / or 14051746-1 - A mutation at position 391 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 391, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 392 of SEQ ID NO: 32 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 392, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 352 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 352, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K352A at position 352 of SEQ ID NO: 33; and / or - A mutation at position 356 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 356, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 357 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 357, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E357A at position 357 of SEQ ID NO: 33; and / or - A mutation at position 358 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 358, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is K358A at position 358 of SEQ ID NO: 33; and / or - A mutation at position 359 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F 14051746-1 residue at position 359, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 360 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 360, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 361 SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 361, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D361A at position 361 of SEQ ID NO: 33; and / or - A mutation at position 372 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 372, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 373 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 373, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; and / or - A mutation at position 374 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 374, more preferably a R for a negatively charged or neutral amino acid, more preferably R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 375 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 375, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 376 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 376, more preferably a G for a positively charged or negatively charged amino acid; and / or 14051746-1 - A mutation at position 377 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 377, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 388 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 388, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 389 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 389, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 390 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 390, more preferably a Q for a negatively charged or positively charged amino acid; and / or - A mutation at position 391 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 391, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 392 of SEQ ID NO: 33 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 392, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 329 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 329, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In 14051746-1 one embodiment, the mutation is K329A at position 329 of SEQ ID NO: 34 or 36; and / or - A mutation at position 333 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 333, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 334 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 334, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E334A at position 334 of SEQ ID NO: 34 or 36; and / or - A mutation at position 335 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 335, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is R335A at position 335 of SEQ ID NO: 34 or 36; and / or - A mutation at position 336 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 336, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 337 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 337, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 338 SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 338, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D338A at position 338 of SEQ ID NO: 34 or 36; and / or - A mutation at position 349 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 349, more preferably a R for a negatively charged or neutral 14051746-1 amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 350 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 350, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; and / or - A mutation at position 351 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 351, more preferably a K for a negatively charged or neutral amino acid, more preferably K for a neutral amino acid, such as A, G or L; and / or - A mutation at position 352 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 352, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 353 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G residue at position 353, more preferably a G for a positively charged or negatively charged amino acid; and / or - A mutation at position 354 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 354, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; and / or - A mutation at position 365 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 365, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 366 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 366, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 367 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q 14051746-1 residue at position 367, more preferably a Q for a negatively charged or positively charged amino acid; and / or - A mutation at position 368 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 368, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 369 of SEQ ID NO: 34 or 36 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 369, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is selected from one or more of the following mutations: - A mutation at position 264 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of the K residue at position 264, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is K264A at position 264 of SEQ ID NO: 35; and / or - A mutation at position 268 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the T residue at position 268, more preferably a T for a positively charged or negatively charged amino acid; and / or - A mutation at position 269 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the substitution is a substitution of the E residue at position 269, for a positively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is E269A at position 269 of SEQ ID NO: 35; and / or - A mutation at position 270 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 270, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; In one embodiment, the mutation is R270A at position 270 of SEQ ID NO: 35; and / or 14051746-1 - A mutation at position 271 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a F residue at position 271, more preferably a F for a negatively charged or positively charged amino acid; and / or - A mutation at position 272 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 272, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 273 SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a D residue at position 273, more preferably a D for a negatively charged or neutral amino acid, more preferably a D for a neutral amino acid, such as A, G or L. In one embodiment, the mutation is D273A at position 273 of SEQ ID NO: 35; and / or - A mutation at position 284 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 284, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 285 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a N residue at position 285, more preferably a N for a negatively charged or neutral amino acid, more preferably a N for a neutral amino acid, such as A, G or L; and / or - A mutation at position 286 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 286, more preferably a K for a negatively charged or neutral amino acid, more preferably K for a neutral amino acid, such as A, G or L; and / or - A mutation at position 287 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 287, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 288 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a G 14051746-1 residue at position 288, more preferably a G for a positively charged or negatively charged amino acid; and / or - A mutation at position 289 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a K residue at position 289, more preferably a K for a negatively charged or neutral amino acid, more preferably a K for a neutral amino acid, such as A, G or L; and / or - A mutation at position 300 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a R residue at position 300, more preferably a R for a negatively charged or neutral amino acid, more preferably a R for a neutral amino acid, such as A, G or L; and / or - A mutation at position 301 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a L residue at position 301, more preferably a L for a negatively charged or positively charged amino acid; and / or - A mutation at position 302 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Q residue at position 302, more preferably a Q for a negatively charged or positively charged amino acid; and / or - A mutation at position 303 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a Y residue at position 303, more preferably a Y for a negatively charged or positively charged amino acid; and / or - A mutation at position 304 of SEQ ID NO: 35 or a corresponding position in a homologous sequence, wherein preferably the mutation is a substitution of a E residue at position 304, more preferably a E for a negatively charged or neutral amino acid, more preferably a E for a neutral amino acid, such as A, G or L. In one embodiment, the stomatal voltage-gated potassium channel is SKOR. Specific embodiments in respect of SKOR channels are described below: In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at positon 334 of SEQ ID NO: 1, 14051746-1 preferably is a substitution of E334 to a neutral amino acid, or a corresponding position in a corresponding mutation. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at positon 338 of SEQ ID NO: 1, preferably is a substitution of D338 to a neutral amino acid, most preferably is D338A, or a corresponding position in a corresponding mutation. In one embodiment, the mutation in the C-linker domain is at least two mutations at positions selected from E334 and D338 of SEQ ID NO: 1 or at least two corresponding positions in a homologous sequence. In one embodiment, the mutation in the N-terminal cytosolic domain is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and the mutation in the C-linker domain is at least two mutations at positions selected from: ^ Position E334 and D338 of SEQ ID NO: 11; ^ position E335 and D339 of SEQ ID NO: 13; ^ position E336 and D340 of SEQ ID NO: 15; ^ position E358 and D362 of SEQ ID NO: 17; ^ position E400 and D404 of SEQ ID NO: 31; ^ position E357 and D361 of SEQ ID NO: 32 or 33; ^ position E334 and D338 of SEQ ID NO: 34; ^ position E269 and D273 of SEQ ID NO: 35; ^ position E334 and D338 of SEQ ID NO: 36; or ^ position E7 and D11 of SEQ ID NO: 38 wherein preferably the mutation is a substitution to a neutral amino acid such as A, G or L, most preferably is E>A and D>A mutation. In one embodiment, any of the described mutations increases the rate of stomatal opening and closing compared in a plant compared to the rate of stomatal opening and closing in a wild-type or control plant. 14051746-1 The plant may be produced by any of the below-described methods. Preferably the mutation is introduced into at least one plant cell and a plant regenerated from the at least one mutated plant cell. In an alternative aspect, the plant comprises and expresses at least one nucleic acid construct, wherein the nucleic acid construct comprises a nucleic acid sequence encoding a GORK channel, selected from SEQ ID NO: 26, 28 and 30 or a functional variant or homologue thereof. In one embodiment, the plant comprises and expresses at least one nucleic acid construct, wherein the nucleic acid construct comprises a nucleic acid sequence comprising a GORK nucleic acid sequence, selected from SEQ ID NO: 25, 27 and 20 or a functional variant or homologue thereof. Preferably, the nucleic acid sequences are operably linked to a regulatory sequence, such as a constitutive, strong or tissue-specific (e.g. stomata-specific) promoter. The nucleic acid constructs may be introduced into a plant by transformation, as described in further detail below. In an alternative aspect, the plant comprises and expresses at least one nucleic acid construct, wherein the nucleic acid construct comprises a nucleic acid sequence encoding a voltage-gated potassium channel, selected from SEQ ID NO: 49, 50, 51, 52, 53 or 54 or a functional variant or homologue thereof. Preferably, the nucleic acid sequences are operably linked to a regulatory sequence, wherein the regulatory sequence may be a constitutive, strong or tissue-specific (e.g. stomata-specific) promoter. The nucleic acid constructs may be introduced into a plant by any known transformation, examples of which are described in further detail below. Preferably, the plant is soybean and the plant comprises and expressing at least one nucleic acid construct, wherein the nucleic acid construct comprises a nucleic acid sequence comprising a voltage-gated potassium channel nucleic acid sequence selected from SEQ ID NO: 50 and / or 51 or a functional variant thereof. Preferably, the plant is maize and the plant comprising and expressing at least one nucleic acid construct, wherein the nucleic acid construct comprises a nucleic acid sequence comprising a voltage-gated potassium channel nucleic acid sequence selected from SEQ ID NO: 52, 53 and / or 54 or a functional variant thereof. 14051746-1 In another aspect of the invention, there is also provided an isolated plant cell transfected with at least one nucleic acid construct as defined herein. Also described is a nucleic acid construct comprising a nucleic acid sequence encoding a voltage-gated potassium channel comprising at least one mutation, wherein the mutation is selected from one of the above-described mutations. Preferably the mutation is a substitution mutation. More preferably, it is a substitution mutation from a positively charged amino acid to a negatively charged or neutral amino acid. Most preferably the mutation is a substitution to neutral amino acid, selected from A, G or L. In a preferred embodiment, the at least one mutation is a mutation at a position selected from 312, 316, 317, 318, 319, 320, 321, 332, 333, 334, 335, 336, 337, 348, 349, 350, 351, 352 and / or 356 of SEQ ID NO: 1, or corresponding position in a homologous sequence, wherein the mutation is not at position 313 of SEQ ID NO: 1. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E317 and D321 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312 and E317 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312 and D321 of SEQ ID NO: 1. In another embodiment, the mutation is a mutation of K312, E317 and D321 of SEQ ID NO:1. In all embodiments, the mutation is not a substitution mutation at position 313 of SEQ ID NO: 1. In another embodiment, the at least one mutation is a mutation at a position selected from a. 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434, 435 of SEQ ID NO: 31; or b. 352, 356, 357, 358, 359, 360, 361, 372, 373, 374, 375, 376, 377, 388, 389, 390, 391, 392 of SEQ ID NO: 33; or c. 353, 357, 358, 359, 360, 361, 362, 373, 374, 375, 376, 377, 378, 389, 390, 391, 392, 393 of SEQ ID NO: 17. 14051746-1 In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E400 and D404 of SEQ ID NO: 31. In another embodiment, the mutation is a mutation of K395 and E400 of SEQ ID NO: 31. In another embodiment, the mutation is a mutation of K395 and D404 of SEQ ID NO: 31. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K395, E400 and D404 of SEQ ID NO: 31. In one embodiment, the mutation may not be a substitution mutation at position 396 of SEQ ID NO: 31. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E357 and D361 of SEQ ID NO: 33. In another embodiment, the mutation is a mutation of K352 and E357 of SEQ ID NO: 33. In another embodiment, the mutation is a mutation of K352 and D361 of SEQ ID NO: 33. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K352, E357 and D361 of SEQ ID NO: 33. In one embodiment, the mutation may not be a substitution mutation at position 353 of SEQ ID NO: 33. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E358 and D362 of SEQ ID NO: 17. In another embodiment, the mutation is a mutation of K353 and E358 of SEQ ID NO: 17. In another embodiment, the mutation is a mutation of K353 and D362 of SEQ ID NO: 17. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K353, E358 and D362 of SEQ ID NO: 17. In one embodiment, the mutation may not be a substitution mutation at position 354 of SEQ ID NO: 17. In another embodiment, the at least one mutation is a mutation at a position selected from a. 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434, 435 of SEQ ID NO: 34 or 36; or 14051746-1 b. 264, 268, 269, 270, 271, 272, 273, 284, 285, 286, 287, 288, 289, 300, 301, 302, 303, 304 of SEQ ID NO: 35. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E334 and D338 of SEQ ID NO: 34 or 36. In another embodiment, the mutation is a mutation of K329 and E334 of SEQ ID NO: 34 or 36. In another embodiment, the mutation is a mutation of K329 and D338 of SEQ ID NO: 34 or 36. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation is a mutation of K329, E334 and D338 of SEQ ID NO: 34 or 36. In one embodiment, the mutation may not be a substitution mutation at position 330 of SEQ ID NO: 34 or 36. In one embodiment, the mutation may comprise at least two mutations selected from the above mutations. In one embodiment, the mutation is a mutation of E269 and D273 of SEQ ID NO: 35. In another embodiment, the mutation is a mutation of K264 and E269 of SEQ ID NO: 35. In another embodiment, the mutation is a mutation of K264 and D273 of SEQ ID NO: 35. In another embodiment, the mutation may comprise at least three mutations selected from the above mutations. In one embodiment, the mutation may comprise a deletion of residues 2-23 of the N- terminal. The Applicant has identified another combination of mutations, referred to as Omni- GORK-2, comprising the combination of a mutation in the S2 domain and also in the N- terminal domain. Specifically, a mutation at F108 in the S2 domain and a deletion of residues 2-23 of the N-terminus domain. Figure 25 B, F, G and H show that this combination has a synergistic effect on thee deactivation time of a channel compared to a channel comprising a mutation in either the S2 or N-terminal domain only. Accordingly, in one embodiment, mutation may comprise a first mutation in the N- terminal cytosolic domain, wherein the mutation is the deletion of the residues 2-23, 14051746-1 preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and a second mutation in the S2 domain at position 108 of SEQ ID NO: 1 or a corresponding position in a homologous sequence. Preferably, the second mutation is a substitution of the F residue at position 108, more preferably a F for a negatively charged or neutral amino acid, more preferably a F for a neutral amino acid, such as A, G or L or S. In one embodiment, the second mutation is F108S at position 108 of SEQ ID NO: 1. The residue F108 first identified in GORK corresponds to position 125 in SEQ ID NO: 11, i.e., the SKOR channel. Accordingly, in one embodiment, mutation may comprise a first mutation in the N-terminal cytosolic domain, wherein the mutation is the deletion of the residues 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal, and a second mutation in the S2 domain at position 125 of SEQ ID NO: 11 or a corresponding position in a homologous sequence. Preferably, the second mutation is a substitution of the F residue at position 125, more preferably a F for a negatively charged or neutral amino acid, more preferably a F for a neutral amino acid, such as A, G or L or S. In one embodiment, the second mutation is F125S at position 108 of SEQ ID NO: 11. Also provided is use of the construct described above, to increase at least one of growth, yield, drought tolerance, water use efficiency and / or carbon assimilation in a plant. In an alternative embodiment, the described construct is used to alter the kinetics of a stomatal voltage-gated potassium channel, wherein a change in channel kinetics is preferably selected from a change in sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage- sensitive ion channel (I). Accordingly, there is also provided use of the construct in a method to produce a plant showing altered stomatal voltage-gated potassium channel kinetics and / or an increase in at least one of growth, yield, drought tolerance, water use efficiency and / or carbon assimilation in a plant. In another aspect of the invention, there is provided a method of increasing or accelerating stomatal conductance and / or the rate of stomatal opening and closing in a plant, the method comprising introducing at least at least of the above-described 14051746-1 mutations into a stomatal voltage-gated potassium channel. Enhancing the rate at which stomata open and close can promote photosynthetic carbon assimilation and water use efficiency (WUE). In one embodiment, the sensitivity of the channel to external potassium is increased at least one-fold, two-fold, three-fold, four-fold, five-fold or more compared to a wild-type or control channel. In another aspect of the invention there is provided a method of increasing at least one of yield, water use efficiency (WUE) and / or carbon assimilation in a plant, the method comprising introducing at least at least one of the above-described mutations, into a stomatal voltage-gated potassium channel. In one embodiment, the method is an increase in WUE without a loss in C assimilation. As shown in Figure 5, by mutating a GORK channel as described herein, the total dry biomass of the GORKkN-gS1-L4and GORKNPplants were enhanced 3.6±0.1- and 2.8±0.3-fold compared to controls under varying light, which translated to a highly significant improvement in WUE of 2.3±0.1- and 1.8±0.2-fold, respectively, when compared to the wild-type plants grown under the fixed light regime (Fig.5f). The term "yield" in general means a measurable produce of economic value, typically related to a specified crop, to an area, and to a period of time. Individual plant parts directly contribute to yield based on their number, size and / or weight. The actual yield is the yield per square meter for a crop per year, which is determined by dividing total production per year (includes both harvested and appraised production) by planted square metres. In one embodiment, the increase in yield is an increase in biomass or dry biomass. An increase in biomass can be measured by assessing any one or more of the following: (a) increased biomass (weight) of one or more parts of a plant, aboveground (harvestable parts), or increased root biomass, increased root volume, increased root length, increased root diameter or increased root length or increased biomass of any other harvestable part. Increased biomass may be expressed as g / plant or kg / hectare or (b) increased seed yield per plant, which may comprise one or more of an increase in seed biomass (weight) per plant or on an individual basis. All parameters are relative to a wild- type or control plant. The terms “seed” and “grain” as used herein can be used interchangeably. The terms "increase", "improve" or "enhance" as used herein are also interchangeable. In one embodiment, an increase in yield comprises at least an increase 14051746-1 in biomass, and in one embodiment, said increase in biomass is at least one-fold, two- fold, three-fold or four-fold or more compared to a wild-type or control plant. By “water use efficiency” or “WUE” is meant the ratio of water used in plant metabolism to water lost through transpiration. In one example, WUE may be measured by measuring the amount of carbon fixed per water transpired. Alternatively, WUE may be measured by measuring the biomass per water transpired over a growing period or the amount of water fed to a plant. Other methods for measuring WUE would be well known to the skilled person. By “carbon assimilation” or carbon fixation (such terms may be used interchangeably) is meant the conversion of inorganic carbon to organic compound, for example, through photosynthesis. In one example, carbon assimilation may be measured by measuring total biomass over time. An “increase” as used herein, may refer to an increase of at least 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90 or 95% or more compared to a control plant. Alternatively, the increase may at least a one-fold two-fold, three-fold, four-fold or five-fold increase, and preferably, between a one-fold and four- fold increase compared to a wild-type or control plant. The increases observed may be under light-fluctuating light conditions. In an alternative embodiment, the method comprises introducing at least one mutation, as described above, into at least one, preferably endogenous, gene encoding a stomatal voltage-gated potassium channel. By “at least one mutation” is means that where the stomatal voltage-gated potassium channel gene is present as more than one copy or homeologue (with the same or slightly different sequence) there is at least one mutation in at least one gene. Preferably all genes are mutated. In one embodiment, the mutation is introduced using mutagenesis or targeted genome editing. That is, in one embodiment, the invention relates to a method and plant that has been generated by genetic engineering methods as described, and does not encompass naturally occurring varieties. 14051746-1 Targeted genome modification or targeted genome editing is a genome engineering technique that uses targeted DNA double-strand breaks (DSBs) to stimulate genome editing through homologous recombination (HR)-mediated recombination events. To achieve effective genome editing via introduction of site-specific DNA DSBs, four major classes of customisable DNA binding proteins can be used: meganucleases derived from microbial mobile genetic elements, ZF nucleases based on eukaryotic transcription factors, transcription activator-like effectors (TALEs) from Xanthomonas bacteria, and the RNA-guided DNA endonuclease Cas9 from the type II bacterial adaptive immune system CRISPR (clustered regularly interspaced short palindromic repeats). Meganuclease, ZF, and TALE proteins all recognize specific DNA sequences through protein-DNA interactions. Although meganucleases integrate nuclease and DNA-binding domains, ZF and TALE proteins consist of individual modules targeting 3 or 1 nucleotides (nt) of DNA, respectively. ZFs and TALEs can be assembled in desired combinations and attached to the nuclease domain of FokI to direct nucleolytic activity toward specific genomic loci. A preferred genome editing method that can be used according to the various aspects of the invention is CRISPR. The use of this technology in genome editing is well described in the art, for example in US 8,697,359 and references cited herein One major advantage of the CRISPR-Cas9 system, as compared to conventional gene targeting and other programmable endonucleases is the ease of multiplexing, where multiple genes can be mutated simultaneously simply by using multiple sgRNAs each targeting a different gene. In addition, where two sgRNAs are used flanking a genomic region, the intervening section can be deleted or inverted (Wiles et al., 2015). Cas9 is thus the hallmark protein of the type II CRISPR-Cas system, and is a large monomeric DNA nuclease guided to a DNA target sequence adjacent to the PAM (protospacer adjacent motif) sequence motif by a complex of two noncoding RNAs: CRISPR RNA (crRNA) and trans-activating crRNA (tracrRNA). The Cas9 protein contains two nuclease domains homologous to RuvC and HNH nucleases. The HNH nuclease domain cleaves the complementary DNA strand whereas the RuvC-like domain cleaves the non-complementary strand and, as a result, a blunt cut is introduced in the target DNA. Heterologous expression of Cas9 together with an sgRNA can 14051746-1 introduce site-specific double strand breaks (DSBs) into genomic DNA of live cells from various organisms. For applications in eukaryotic organisms, codon optimized versions of Cas9, which is originally from the bacterium Streptococcus pyogenes, have been used. The single guide RNA (sgRNA) is the second component of the CRISPR / Cas system that forms a complex with the Cas9 nuclease. sgRNA is a synthetic RNA chimera created by fusing crRNA with tracrRNA. The sgRNA guide sequence located at its 5′ end confers DNA target specificity. Therefore, by modifying the guide sequence, it is possible to create sgRNAs with different target specificities. The canonical length of the guide sequence is 20bp. In plants, sgRNAs have been expressed using plant RNA polymerase III promoters, such as U6 and U3. Accordingly, using techniques known in the art it is possible to design sgRNA molecules that target the GORK sequence, and in particular, the cytosolic N-termini and / or the C-linker domain as described herein. In one embodiment, the sgRNA molecules target a sequence selected from SEQ ID No: 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43 or a variant thereof as defined herein. Cas9 expression plasmids for use in the methods of the invention can be constructed as described in the art. In a preferred embodiment of any aspect of the invention described herein, sgRNA can be used with a modified Cas9 protein, such as nickase Cas9 or nCas9 or a “dead” Cas9 (dCas9) fused to a “Base Editor” – such as an enzyme, for example a deaminase such as cytidine deaminase, or TadA (tRNA adenosine deaminase) or ADAR or APOBEC. These enzymes are able to substitute one base for another. As a result no DNA is deleted, but a single substitution is made (Kim et al., 2017; Gaudelli et al. 2017). Alternatively, the method may use sgRNA together with a template or donor DNA construct, to introduce a targeted substitution, and in particular one of the substitutions described herein. In this embodiment, the introduction of a template DNA strand, following a sgRNA-mediated snip in the double-stranded DNA, can be used to produce a specific targeted mutation in the gene using homology directed repair. As a further alternative, prime editing can be used to introduce the specific mutation (Anzalone et al., 2019). Here a catalytically impaired Cas9 endonuclease is fused to an engineered reverse transcriptase programmed with a prime editing guide RNA (pegRNA) that is both specific to the target site and encodes the desired edit. 14051746-1 In an alternative embodiment, the nuclease used may be Cpf1 or MAD7. Another genome editing system that may be used is the Fanzor system (see Saito, M., Xu, P., Faure, G. et al. Fanzor is a eukaryotic programmable RNA-guided endonuclease. Nature (2023)). Here, nearby noncoding RNAs (ωRNAs) can be used with the Fanzor endonuclease to introduce insertions / deletions at targeted sites. Other genome editing systems that can be used also include the prokaryotic OMEGA / TnpB system (Karvelis T, Druteika G, Bigelyte G, Budre K, Zedaveinyte R, Silanskas A, Kazlauskas D, Venclovas Č, Siksnys V. Transposon-associated TnpB is a programmable RNA-guided DNA endonuclease. Nature.2021 Nov;599(7886):692-696). Alternatively, more conventional mutagenesis methods can be used to introduce at least one mutation into stomatal voltage-gated potassium channel. These methods include both chemical and physical mutagenesis. Examples include T-DNA mutagenesis and targeting induced local lesions in genomes (TILLING). These techniques are well known in the art. Furthermore, rapid high-throughput screening procedures allow the analysis of amplification products for identifying a mutation in the potassium channel as described above, as compared to a corresponding non-mutagenised wild type plant. Once a mutation is identified in a gene of interest, the seeds of the M2 plant carrying that mutation are grown into adult M3 plants and screened for an alteration in stomatal kinetics. Plants and plant parts obtained or obtainable by the methods described above which carry the above described nucleic acid constructs or carry a functional mutation in the potassium channel also within the scope of the invention. In a further aspect of the invention there is provided a method of producing a plant with an increase in at least one of growth, yield, water use efficiency and / or carbon assimilation compared to a control plant, the method comprising introducing on or more of the above-described mutations into the plant. Accordingly, in one embodiment, the method comprises a. selecting a part of the plant; b. transfecting at least one cell of the part of the plant of paragraph (a) with at least one sgRNA (designed as described above); 14051746-1 c. regenerating at least one plant derived from the transfected cell or cells; d. selecting one or more plants obtained according to paragraph (c) that have one or more mutations in the potassium channel, and preferably, in the C- linker domain and / or the cytosolic N termini of the channel. Any of the genome editing constructs or nucleic acid constructs described herein, may be introduced into said plant through a process called transformation. The term "introduction" or "transformation" as referred to herein encompasses the transfer of an exogenous polynucleotide into a host cell, irrespective of the method used for transfer. Plant tissue capable of subsequent clonal propagation, whether by organogenesis or embryogenesis, may be transformed with a genetic construct of the present invention and a whole plant regenerated there from. The particular tissue chosen will vary depending on the clonal propagation systems available for, and best suited to, the particular species being transformed. Exemplary tissue targets include leaf disks, pollen, embryos, cotyledons, hypocotyls, megagametophytes, callus tissue, existing meristematic tissue (e.g., apical meristem, axillary buds, and root meristems), and induced meristem tissue (e.g., cotyledon meristem and hypocotyl meristem). The polynucleotide may be transiently or stably introduced into a host cell and may be maintained non-integrated, for example, as a plasmid. Alternatively, it may be integrated into the host genome. The resulting transformed plant cell may then be used to regenerate a transformed plant in a manner known to persons skilled in the art. The transfer of foreign genes into the genome of a plant is called transformation. Transformation of plants is now a routine technique in many species. Advantageously, any of several transformation methods may be used to introduce the gene of interest into a suitable ancestor cell. The methods described for the transformation and regeneration of plants from plant tissues or plant cells may be utilized for transient or for stable transformation. Transformation methods include the use of liposomes, electroporation, chemicals that increase free DNA uptake, injection of the DNA directly into the plant, particle gun bombardment, transformation using viruses or pollen and microprojection. Methods may be selected from the calcium / polyethylene glycol method for protoplasts, electroporation of protoplasts, microinjection into plant material, DNA or RNA-coated particle bombardment, infection with (non-integrative) viruses and the like. Transgenic plants, including transgenic crop plants, are preferably produced via Agrobacterium tumefaciens mediated transformation. According to the invention, the nucleic acid is 14051746-1 preferably stably integrated in the transgenic plants genome and the progeny of said plant therefore also comprises the transgene. To select transformed plants, the plant material obtained in the transformation is, in certain embodiments, subjected to selective conditions so that transformed plants can be distinguished from untransformed plants. For example, the seeds obtained in the above-described manner can be planted and, after an initial growing period, subjected to a suitable selection by spraying. A further possibility is growing the seeds, if appropriate after sterilization, on agar plates using a suitable selection agent so that only the transformed seeds can grow into plants. Alternatively, the transformed plants are screened for the presence of a selectable marker such as the ones described above. Following DNA or nucleic acid transfer and regeneration, putatively transformed plants may also be evaluated, for instance using Southern analysis, for the presence of one or more of the above-described mutations. The generated transformed plants may be propagated by a variety of means, such as by clonal propagation or classical breeding techniques. For example, a first generation (or T1) transformed plant may be selfed and homozygous second-generation (or T2) transformants selected, and the T2plants may then further be propagated through classical breeding techniques. The generated transformed organisms may take a variety of forms. For example, they may be chimeras of transformed cells and non-transformed cells; clonal transformants (e.g., all cells transformed to contain the expression cassette); grafts of transformed and untransformed tissues (e.g., in plants, a transformed rootstock grafted to an untransformed scion). In a further embodiment of any of the methods described herein, the method may further comprise at least one or more of the steps of assessing the phenotype of the genetically altered plant, measuring at least one of an increase in at least one of growth, yield, water use efficiency and / or carbon assimilation and comparing said phenotype to determine an increase in at least one of growth, yield, water use efficiency and / or carbon assimilation in a wild-type or control plant. In other words, the method may involve the step of screening the plants for the desired phenotype. 14051746-1 In a further aspect of the invention, there is provided a method of screening a population of plants and identifying and / or selecting a plant that will have at least one of altered rate of altered stomatal closure rate, increased water use efficiency, increased carbon assimilation, as described herein, compared to a control or wild-type plant, the method comprising detecting at least one of the above described polymorphisms or at least one of the above-described mutations in the N-terminal domain, C-linker domain or in both the N-terminal and C-linker domains of a voltage-gated potassium channel gene, preferably selected from GORK or SKOR or KOR, wherein said mutation or polymorphism leads to an alteration in the channel kinetics of the stomatal voltage-gated potassium channel, wherein an alteration in channel kinetics is preferably selected from a change in sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage-sensitive ion channel (I). In a further aspect of the invention, there is provided a method of screening a population of plants and identifying and / or selecting a plant that has an alteration in channel kinetics of a stomatal voltage-gated potassium channel, wherein an alteration in channel kinetics is preferably selected from a change in sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage- sensitive potassium channel (I) in a plant as described herein, compared to a control or wild-type plant, the method comprising detecting at least one at least one of the above described polymorphisms or at least one of the above-described mutations in the N- terminal domain or C-linker domain or in both the N-terminal and C-linker domains of a voltage-gated potassium channel gene, preferably selected from GORK or SKOR or KOR, wherein said mutation or polymorphism leads to an alteration in the channel kinetics of the stomatal voltage-gated potassium channel. In one embodiment, the plant may be further characterised by an altered rate of stomatal closure, increased water use efficiency and / or increased carbon assimilation. Suitable tests for assessing the presence of a polymorphism would be well known to the skilled person, and include but are not limited to, Isozyme Electrophoresis, Restriction Fragment Length Polymorphisms (RFLPs), Randomly Amplified Polymorphic DNAs (RAPDs), Arbitrarily Primed Polymerase Chain Reaction (AP-PCR), DNA Amplification Fingerprinting (DAF), Sequence Characterized Amplified Regions (SCARs), Amplified Fragment Length polymorphisms (AFLPs), Simple Sequence Repeats (SSRs-which are 14051746-1 also referred to as Microsatellites), and Single Nucleotide Polymorphisms (SNPs). In one embodiment, Kompetitive Allele Specific PCR (KASP) genotyping is used. A method may also comprise the step of assessing whether the polymorphism has an effect on voltage-gated potassium channel kinetics or stomatal closure or water use efficiency or carbon assimilation as described herein. Methods to screen for an effect on stomatal conductance are described in example VII of the application. In one embodiment, the method comprises a) obtaining a nucleic acid sample from a plant and b) carrying out nucleic acid amplification of one or more GORK or SKOR or KOR gene and / or promoter alleles using one or more primer pairs. In a further aspect of the invention there is provided a method of altering rate of stomatal closure or altering water use efficiency or carbon assimilation in a plant, as described above in a plant, the method comprising a. screening a population of plants for at least one plant with at least one of the above described polymorphisms or mutations; and b. introducing at least one further polymorphism or mutation described above in to a voltage-gated potassium channel, preferably selected from GORK or SKOR or KOR. In a further aspect of the invention there is provided a plant obtained or obtainable by the above described methods. The term “variant” or “functional variant” as used throughout with reference to any of the sequences described herein refers to a variant gene sequence or part of the gene sequence (such as a fragment) which retains the biological function of the full non-variant sequence – i.e. the variant is able to act as a K+efflux channel. A functional variant also comprises a variant of the gene of interest, which has sequence alterations that do not affect function, for example in non-conserved residues. Also encompassed is a variant that is substantially identical, i.e. has only some sequence variations, for example in non- conserved residues, compared to the wild type sequences as shown herein and is biologically active. Alterations in a nucleic acid sequence that results in the production of a different amino acid at a given site that does not affect the functional properties of the 14051746-1 encoded polypeptide are well known in the art. For example, a codon for the amino acid alanine, a hydrophobic amino acid, may be substituted by a codon encoding another less hydrophobic residue, such as glycine, or a more hydrophobic residue, such as valine, leucine, or isoleucine. Similarly, changes which result in substitution of one negatively charged residue for another, such as aspartic acid for glutamic acid, or one positively charged residue for another, such as lysine for arginine, can also be expected to produce a functionally equivalent product. Each of the proposed modifications is well within the routine skill in the art, as is determination of retention of biological activity of the encoded products. As used in any aspect of the invention described throughout a “variant” or a “functional variant” has at least 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% overall sequence identity to the non-variant nucleic acid or amino acid sequence. Two nucleic acid sequences or polypeptides are said to be "identical" if the sequence of nucleotides or amino acid residues, respectively, in the two sequences is the same when aligned for maximum correspondence as described below. The terms "identical" or percent "identity," in the context of two or more nucleic acids or polypeptide sequences, refer to two or more sequences or subsequences that are the same or have a specified percentage of amino acid residues or nucleotides that are the same, when compared and aligned for maximum correspondence over a comparison window, as measured using one of the following sequence comparison algorithms or by manual alignment and visual inspection. When percentage of sequence identity is used in reference to proteins or peptides, it is recognised that residue positions that are not identical often differ by conservative amino acid substitutions, where amino acids residues are substituted for other amino acid residues with similar chemical properties (e.g., charge or hydrophobicity) and therefore do not change the functional properties of the molecule. Where sequences differ in conservative substitutions, the percent sequence identity may be adjusted upwards to correct for the conservative nature of the substitution. Means for making this adjustment are well known to those of skill in the art. For sequence 14051746-1 comparison, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Default program parameters can be used, or alternative parameters can be designated. The sequence comparison algorithm then calculates the percent sequence identities for the test sequences relative to the reference sequence, based on the program parameters. Non-limiting examples of algorithms that are suitable for determining percent sequence identity and sequence similarity are the BLAST and BLAST 2.0 algorithms. Suitable homologues can be identified by sequence comparisons and identifications of conserved domains. There are predictors in the art that can be used to identify such sequences. The function of the homologue can be identified as described herein and a skilled person would thus be able to confirm the function, for example when overexpressed in a plant. By corresponding position in a homologous sequence is meant, an analogous and / or a functionally equivalent position within a sequence. That is, the corresponding position may be at a different residue number, but within the equivalent domain or motif within a given sequence. In many, but not all, cases, the charge of the corresponding residue is conserved. Thus, the nucleotide sequences of the invention and described herein can also be used to isolate corresponding sequences from other organisms, particularly other plants, for example crop plants. In this manner, methods such as PCR, hybridization, and the like can be used to identify such sequences based on their sequence homology to the sequences described herein. Topology of the sequences and the characteristic domains structure can also be considered when identifying and isolating homologs. Sequences may be isolated based on their sequence identity to the entire sequence or to fragments thereof. In hybridization techniques, all or part of a known nucleotide sequence is used as a probe that selectively hybridizes to other corresponding nucleotide sequences present in a population of cloned genomic DNA fragments or cDNA fragments (i.e., genomic or cDNA libraries) from a chosen plant. The hybridization probes may be genomic DNA fragments, cDNA fragments, RNA fragments, or other oligonucleotides, 14051746-1 and may be labelled with a detectable group, or any other detectable marker. Methods for preparation of probes for hybridization and for construction of cDNA and genomic libraries are generally known in the art and are disclosed in Sambrook, et al., (1989) Molecular Cloning: A Library Manual (2d ed., Cold Spring Harbor Laboratory Press, Plainview, New York). Hybridization of such sequences may be carried out under stringent conditions. By "stringent conditions" or "stringent hybridization conditions" is intended conditions under which a probe will hybridize to its target sequence to a detectably greater degree than to other sequences (e.g., at least 2-fold over background). Stringent conditions are sequence dependent and will be different in different circumstances. By controlling the stringency of the hybridization and / or washing conditions, target sequences that are 100% complementary to the probe can be identified (homologous probing). Alternatively, stringency conditions can be adjusted to allow some mismatching in sequences so that lower degrees of similarity are detected (heterologous probing). Generally, a probe is less than about 1000 nucleotides in length, preferably less than 500 nucleotides in length. Typically, stringent conditions will be those in which the salt concentration is less than about 1.5 M Na ion, typically about 0.01 to 1.0 M Na ion concentration (or other salts) at pH 7.0 to 8.3 and the temperature is at least about 30°C for short probes (e.g., 10 to 50 nucleotides) and at least about 60°C for long probes (e.g., greater than 50 nucleotides). Duration of hybridization is generally less than about 24 hours, usually about 4 to 12. Stringent conditions may also be achieved with the addition of destabilizing agents such as formamide. A plant according to all aspects of the invention described herein may be a monocot or a dicot plant. Preferably, the plant is a crop plant. By crop plant is meant any plant which is grown on a commercial scale for human or animal consumption or use. In a preferred embodiment, the plant is a cereal. In another embodiment the plant is Arabidopsis. The plant according to the various aspects of the invention may be a moncot or a dicot plant. A dicot plant may be selected from the families including, but not limited to Asteraceae, Brassicaceae (eg Brassica napus), Chenopodiaceae, Cucurbitaceae, Leguminosae (Caesalpiniaceae, Aesalpiniaceae Mimosaceae, Papilionaceae or Fabaceae), Malvaceae, Rosaceae or Solanaceae. For example, the plant may be selected from lettuce, sunflower, Arabidopsis, broccoli, spinach, water melon, squash, 14051746-1 cabbage, tomato, potato, yam, capsicum, tobacco, cotton, okra, apple, rose, strawberry, alfalfa, bean, soybean, field (fava) bean, pea, lentil, peanut, chickpea, apricots, pears, peach, grape vine or citrus species. In one embodiment, the plant is oilseed rape. Also included are biofuel and bioenergy crops such as rape / canola, sugar cane, sweet sorghum, Panicum virgatum (switchgrass), linseed, lupin and willow, poplar, poplar hybrids, Miscanthus or gymnosperms, such as loblolly pine. Also included are crops for silage (maize), grazing or fodder (grasses, clover, sanfoin, alfalfa), fibres (e.g. cotton, flax), building materials (e.g. pine, oak), pulping (e.g. poplar), feeder stocks for the chemical industry (e.g. high erucic acid oil seed rape, linseed) and for amenity purposes (e.g. turf grasses for golf courses), ornamentals for public and private gardens (e.g. snapdragon, petunia, roses, geranium, Nicotiana sp.) and plants and cut flowers for the home (African violets, Begonias, chrysanthemums, geraniums, Coleus spider plants, Dracaena, rubber plant). A monocot plant may, for example, be selected from the families Arecaceae, Amaryllidaceae or Poaceae. For example, the plant may be a cereal crop, such as wheat, rice, barley, maize, oat, sorghum, rye, millet, buckwheat, turf grass, Italian rye grass, sugarcane or Festuca species, or a crop such as onion, leek, yam or banana. Preferably, the plant is a crop plant. By crop plant is meant any plant which is grown on a commercial scale for human or animal consumption or use. Preferred plants are maize, wheat, rice, oilseed rape, sorghum, soybean, potato, tomato, grape, barley, pea, bean, field bean, lettuce, cotton, sugar cane, sugar beet, broccoli or other vegetable brassicas or poplar. In one embodiment, the plant is selected from Brassica, wheat, rice, oil palm, soybean, tomato, potato and pepper, preferably soybean or maize. In a further embodiment the plant is soybean. In an alternative embodiment the plant is maize. The term "plant" as used herein encompasses whole plants, ancestors and progeny of the plants and plant parts, including seeds, fruit, shoots, stems, leaves, roots (including tubers), flowers, tissues and organs, wherein each of the aforementioned comprise the nucleic acid construct as described herein or carry the herein described mutations. The term "plant" also encompasses plant cells, suspension cultures, callus tissue, embryos, 14051746-1 meristematic regions, gametophytes, sporophytes, pollen and microspores, again wherein each of the aforementioned comprises the nucleic acid construct or mutations as described herein. The invention also extends to harvestable parts of a plant of the invention as described herein, but not limited to seeds, leaves, fruits, flowers, stems, roots, rhizomes, tubers and bulbs. The aspects of the invention also extend to products derived, preferably directly derived, from a harvestable part of such a plant, such as dry pellets or powders, oil, fat and fatty acids, starch or proteins. Another product that may be derived from the harvestable parts of the plant of the invention is biodiesel. The invention also relates to food products and food supplements comprising the plant of the invention or parts thereof. In one embodiment, the food products may be animal feed. In another aspect of the invention, there is provided a product derived from a plant as described herein or from a part thereof. In a most preferred embodiment, the plant part or harvestable part is a seed or the fruit. Therefore, in a further aspect of the invention, there is provided a seed or fruit produced from a genetically altered plant as described herein. A control plant as used herein according to all of the aspects of the invention is a plant which has not been modified according to the methods of the invention. Accordingly, in one embodiment, the control plant does not have one or more of the above-described mutations. In one embodiment, the control plant is a wild type plant. The control plant is typically of the same plant species, preferably having the same genetic background as the modified plant. While the foregoing disclosure provides a general description of the subject matter encompassed within the scope of the present invention, including methods, as well as the best mode thereof, of making and using this invention, the following examples are provided to further enable those skilled in the art to practice this invention and to provide a complete written description thereof. However, those skilled in the art will appreciate that the specifics of these examples should not be read as limiting on the invention, the scope of which should be apprehended from the claims and equivalents thereof appended to this disclosure. Various further aspects and embodiments of the present invention will be apparent to those skilled in the art in view of the present disclosure. 14051746-1 "and / or" where used herein is to be taken as specific disclosure of each of the two specified features or components with or without the other. For example "A and / or B" is to be taken as specific disclosure of each of (i) A, (ii) B and (iii) A and B, just as if each is set out individually herein. Unless context dictates otherwise, the descriptions and definitions of the features set out above are not limited to any particular aspect or embodiment of the invention and apply equally to all aspects and embodiments which are described. The foregoing application, and all documents and sequence accession numbers cited therein or during their prosecution ("appln cited documents") and all documents cited or referenced in the appln cited documents, and all documents cited or referenced herein ("herein cited documents"), and all documents cited or referenced in herein cited documents, together with any manufacturer's instructions, descriptions, product specifications, and product sheets for any products mentioned herein or in any document incorporated by reference herein, are hereby incorporated herein by reference, and may be employed in the practice of the invention. More specifically, all referenced documents are incorporated by reference to the same extent as if each individual document was specifically and individually indicated to be incorporated by reference. The invention is now described in the following non-limiting examples. EXAMPLE I: GORK channels interact via the voltage-sensor domain N-terminus We generated VSDs to test whether truncated channel domains would interact with the full-length channel protein, knowing that VSDs are expressed and function on their own in the membrane. The yeast mating-based split-ubiquitin screen (mbSUS) yields growth of the diploid yeast on selective media only when the two halves of the split-ubiquitin moiety are brought together through interaction between putative protein interactors to which they are fused. mbSUS assays enable tests for interaction with full-length membrane proteins and the strength of interaction can be assessed by suppressing the bait protein fusion under the control of a Met-sensitive promoter. We used this screen to assess interactions of the full-length GORK as bait with the VSD of GORK (gVSD) as the prey. Strong growth was 14051746-1 recovered on selective media, even in 500 ^M Met, but growth was not recovered with the VSD of KAT1 (kVSD) or with full-length KAT1 as preys (Fig. 1b). These findings demonstrated an interaction with GORK that was specific to the structure of the gVSD. EXAMPLE II: Interaction depends on a surface of alternating charged residues We carried out sequential domain substitutions in gVSD with the corresponding domains of kVSD in order to identify regions critical for gVSD interaction with GORK. Again, the VSD-GORK interactions were tested by mbSUS assay. Growth of the diploid yeast (Fig. 1c) in the presence of Met was recovered with chimeras that incorporated the cytosolic N-terminus of gVSD, even when the remaining structure was from kVSD. Conversely, interaction was strongly reduced when the N-terminus of gVSD was replaced with the kVSD N-terminus. Some growth was evident without added Met when yeast expressed the kVSD N-terminus in the GORK VSD backbone, specifically with the gVSDkNgS1-L4and gVSDkN-L1gS2-L4preys. This weaker growth was lost when the N-terminus and the cytosolic S2-S3 loop of the gVSD backbone were both replaced with the corresponding kVSD sequences, suggesting the presence of an internal binding site for the VSD N-terminus of the full-length GORK, possibly in the GORK S2-S3 loop. We concluded that the primary site essential for binding was localized within the cytosolic N-terminus of 69 residues of the GORK channel. Both the GORK and KAT1 N-termini harbor similarly charged amino acids in the first 21 residues, diverging thereafter before converging to a near-identical sequence near the base of the S1 α-helix. Deleting the first 23 residues of gVSD had no obvious effect on its interaction with GORK in mbSUS assays, but further truncations failed to recover yeast growth (Fig.7) indicating that residues critical for interaction were situated among the subsequent 39 amino acids preceding the S1 α-helix. However, alanine-scanning mutagenesis of residues 23-66, individually and severally among the most divergent regions within this sequence failed to uncover a clear difference in yeast growth (figure 8), suggesting that interactions between the VSDs of GORK did not depend on a unique amino acid motif. Aligning the N-termini of GORK and related channels of species from Brassica napus to wheat and rice showed a well-conserved pattern of alternating charges beyond the first 20 amino acids (Fig.2a) that is not found in the KAT1 N-terminus (Fig.2b). We reasoned 14051746-1 that this alternation might present a charged surface 'registered' for a zipper-like interaction of the gVSD with a complementary surface on the full-length channel. Indeed, replacing all negatively-charged amino acids (Asp, Glu) with positively-charged residues (Lys) within these domains (gVSDNP) suppressed diploid yeast growth in split-ubiquitin assays; growth was similarly suppressed when all positively-charged residues were replaced with negatively-charged residues (gVSDPN) and when all of the charged residues were substituted with Ala. (gVSDA). However, growth was recovered (Fig.2c) when negatively- and positively-charged residues were exchanged (gVSDPNNP), implying that the alternation in charged surfaces between the domains enables a registration of interactions with a complementarily charged surface to facilitate gVSD binding. To support these findings, we carried out gel filtration analysis for N-terminal multimer assemblies in vitro and assessed VSD–GORK interaction by ratiometric bimolecular fluorescence complementation (rBiFC) in vivo. The in vitro approach offered quantitative information about possible multimer assemblies but was limited necessarily to work with the soluble N-termini. rBiFC analysis enabled a close comparison with the constructs expressed for the mbSUS studies and included internal controls for transformation and transgene loading. However, we did not expect the rBiFC studies to show puncta or a K+ dependency, because VSD binding would ‘cap’ the interacting surfaces of any GORK channel assembly (Fig.1a) and BiFC annealing renders a largely stable complex. Gel filtration measurements showed that the gVSD and gVSDPNNPN-termini eluted at apparent molecular weights near 26 kD, consistent with the formation of dimers as might be expected for inter-molecular binding between adjacent channels (Fig. 1a). By contrast, both the kVSD and gVSDNP N-termini eluted as monomers near 13 kD. Confocal imaging yielded similar results, showing a strong rBiFC signal in vivo on expressing GORK with gVSD and gVSDPNNPbut not with kVSD or the non-interacting mutants gVSDkNgS1-L4and gVSDNP. Thus, the most parsimonious explanation is that an alternation in charged surfaces along the N-termini enables interactions, with a complementarily charged surface between the VSD N-termini of GORK. EXAMPLE III: gVSD interactions affect GORK clustering on transient expression. To assess clustering, initially we introduced a selection of these mutations in the full- length channel tagged with GFP and expressed the constructs transiently in tobacco leaves for confocal image analysis. After mounting, the upper epidermis of leaf segments 14051746-1 was removed and the lower epidermis and remaining mesophyll were superfused with 0.1 mM K+and then with 50 mM K+while imaging. Channel clustering was quantified in the epidermal cells by measuring GFP fluorescence along the cell periphery and calculating the relative standard deviation (RSD) from each of six or more independent experiments. As before, a pronounced redistribution of the punctate GFP fluorescence of the leaf tissue expressing GORKwtwhen transferred from 0.1 mM to 50 mM K+. We observed (figure 9a) a similar K+dependence to clustering for GORKPNNP(SEQ ID NO: 23 and 24), but each of the mutants GORKkN-gS1-L4(SEQ ID NO: 27 and 28), GORKPN(SEQ ID NO: 29 and 30) and GORKNP(SEQ ID NO: 25 and 26) gave little evidence of clustering, even in 0.1 mM K+. Analysis of these experiments (figure 9b) showed a significant decline in RSD with K+elevations for both GORKwtand GORKPNNP; it also showed much reduced RSD values for GORKkN-gS1-L4, GORKPNand GORKNPthat were unaffected by K+concentration, indicating that these mutant forms were dispersed around the cell periphery, their distribution independent of K+outside. Thus, we conclude that the mutations eliminating gVSD binding with GORK also suppress GORK clustering. GORK yields a current under voltage clamp that activates with positive-going voltage steps and decreasing K+outside; as a consequence, the steady-state current-voltage (IV) curve shifts positive-going with increasing external K+. We observed much the same behaviour when GORKwtwas expressed in Xenopus oocytes (figure 10a). Expressing the same clustering-impaired constructs of GORKkN-gS1-L4, GORKPNand GORKNP(figure 10b – d) led to negative-going shifts in the IV curves at each K+concentration relative to GORKwt, but not when positively- and negatively-charged residues were exchanged with the GORKPNNPmutant (figure 10e). The ensemble current of a voltage-sensitive ion channel can be described by a Boltzmann function of the form I = G δF(V-V max (V-EK) / (1+e 1 / 2) / RT) [1] where Gmax is the maximum ensemble conductance, V is the voltage, EK is the equilibrium voltage for K+, F is the Faraday constant, R is the universal gas constant, and T is the temperature. The parameters V1 / 2 and δ define the midpoint voltage for 14051746-1 gating and the sensitivity of the gate to a change in voltage, respectively. To quantify gating, we resolved the ensemble parameters Gmax, V1 / 2 and δ by joint, least-squares fitting to Eqn [1] of the steady-state K+currents across the K+concentrations. In each case, the analysis yielded visually satisfactory fittings with δ held in common and statistically significant shifts in V1 / 2 with K+concentration. However, at any one K+concentration, V1 / 2 values for GORKkN-gS1-L4, GORKPNand GORKNPwere displaced by - 19±2 to -46±5 mV, consistent with a decrease in free energy for gating, ^ ^G, between - 0.23 and -0.92 Kcal / mol. Indeed, plotting V1 / 2 as a function of K+concentration showed that each of the mutants affected in clustering also retained a dependence on K+outside; however, substantially higher K+concentrations were required to achieve a V1 / 2 similar to the GORKwt, indicating 3- to 8-fold decreases in the sensitivity to inhibition by K+(figure 10f). In other words, mutating residues that promoted GORK clustering counterintuitively also appeared to reduce the free energy barrier for gating. EXAMPLE IV: Manipulating GORK alters clustering and enhances K+ currents in guard cells To assess the consequences of the GORK mutations in vivo, we generated stable transformants of GORKwt, GORKkN-gS1-L4, GORKNPand GORKPNNP, again expressing the proteins with GFP tags. Lines were generated under control of the constitutive pUB10 and guard cell-selective pGC1 promoters in the gork null mutant background of Arabidopsis. GORK transgene suppression had previously proven a difficulty, and we therefore analysed the T1 generation, after selecting plants for growth on Basta and GFP fluorescence, and T2 populations from at least three independent transformed lines of these T1 plants. In eight or more experiments with each construct, we observed no appreciable differences between transformants and the results were pooled accordingly. Plants complemented with GORKwtand GORKPNNPshowed a peripheral clustering of the fluorescent marker in 0.1 mM K+that dispersed when K+outside was raised to 50 mM, much as observed in the wild type before. However, plants complemented with the non- interacting GORK mutations exhibited a diffuse distribution of GFP fluorescence around the guard cell periphery, even in 0.1 mM K+, that was unaffected by external K+(Fig.3). We recorded GORK currents under voltage clamp from intact guard cells of the same plants and, as a control, from the gork null mutant background to confirm the lack of outward current. Recordings were carried out over an intermediate range of 14051746-1 concentrations from 1 to 30 mM K+(Fig.4a-e) to expose shifts in K+-dependent gating. As in the oocytes, guard cells of wild-type Arabidopsis and the GORKwtand GORKPNNPcomplemented plants yielded currents that activated positive-going voltage steps and IV curves that were displaced positive-going with increasing external K+. Guard cells of plants complemented with the non-interacting GORK mutations showed similar currents; however, in this case the IV curves were shifted negative-going along the voltage axis at each K+concentration compared to the wild type current and the GORKwttransformants. Mean steady-state currents were well-fitted using the Boltzmann function of Eqn [1] (Fig. 4a-e, solid lines) with a common value for δ but with significant displacements of V1 / 2for the non-interacting mutants. At 30 mM K+, V1 / 2 values for GORKkN-gS1-L4and GORKNPwere displaced by -28±4 and -17±3 mV (Fig.4f) equivalent to ^ ^G values of -0.56 and - 0.20 Kcal / mol and a decrease in sensitivity to K+outside by factors of 7.4±0.9- and 4.5±0.4-fold, respectively, relative to the wild-type and GORKwttransformants. Thus, as in oocytes, each of the non-interacting mutants reduced the inhibition of channel activity by external K+, whereas the GORKPNNPcomplementation rescued the wild-type characteristics. EXAMPLE VI: GORK mutations impact on stomatal dynamics and gas exchange Because the non-interacting mutations enhanced GORK current with voltage and external K+concentration, we anticipated that the effect should be evident as an acceleration in changes of stomatal conductance, gs, following a closing stimulus. Incorporating a -30 mV shift of V1 / 2for GORK in simulations using the OnGuard3 platform predicted an acceleration in gsclosing rates (Fig. 5a). Counterintuitively, they also predicted a small increase in the rate of opening, its dynamic range and steady-state gsthat could be ascribed to an inward conductance and K+uptake through GORK introduced by the shift in V1 / 2(Fig.4 and Fig.11). To test these predictions, we recorded the gas exchange characteristics of the same plants used for the analysis of clustering and channel gating. Experiments incorporated transitions to 200 ^mol m-2s-1photosynthetically-active radiation (PAR) from the dark and back again after preconditioning with 200 ^mol m-2s-1PAR. The results (Fig. 5a-c) confirmed highly significant accelerations of 1.4±0.1- and 1.6±0.2-fold for GORKNPand GORKkN-gS1-L4, respectively, in the rate of gsdecline on transit to dark. They also showed 14051746-1 a small acceleration of opening and increases of 1.1±0.1 and 1.2±0.1-fold in steady-state gs in the light, respectively. One measure of plant performance is water use efficiency (WUE), often defined as the amount of dry mass produced per unit water transpired. WUE is affected by light through the combined influence on carbon demand and associated transpiration. With the enhanced gsand accelerated rates of stomatal movement we reasoned that the effects might translate to increases in WUE and biomass under fluctuating light. Light varies throughout the day in the natural environment, for example as clouds pass by. Photosynthesis generally tracks the energy input of light, but stomata are slower to respond to changes in light intensity, and this difference in kinetics can result in suboptimal assimilation rates when light intensity rises and to transpiration without corresponding assimilation when light intensity falls quickly. Thus, we reasoned that accelerating stomatal closure by manipulating GORK gating might enhance WUE and carbon assimilation when integrated over a period of vegetative growth under fluctuating light. We compared the growth of wild-type plants, the gork null mutant and the gork lines complemented with GORKwt, GORKkN-gS1-L4and GORKNPand GORKPNNPunder control of the pGC1 promoter. The complemented plants were selected as before. All lines were grown together under two light regimes, with plant exposed to a fixed daylight intensity of 140 ^mol m-2s-1PAR or to the same daylight period with varying light and the equivalent total fluence. For the fluctuating light regime, we stepped the light intensity between 10 and 220 ^mol m-2s-1with step intervals of 15 min, thus approximating the times normally required for stomatal closing and roughly half of that for opening. We also limited water availability under both regimes, maintaining soil moisture at 8±4% throughout the 5-week period of growth. Rosette areas, fresh and dry weights of all plants were reduced under fluctuating light compared to the constant daylight conditions. Grown under the fluctuating light, however, the GORKkN-gS1-L4and GORKNPtransgenic plants showed greater rosette areas and dry weights compared to the wild-type control, GORKwtand GORKPNNPlines, and only marginally reduced when compared to plants grown under the fixed light regime (Fig.5d- f). Total dry biomass of the GORKkN-gS1-L4and GORKNPplants were enhanced 3.6±0.1- and 2.8±0.3-fold compared to the controls under varying light, which translated to a 14051746-1 highly significant improvement in WUE of 2.3±0.1- and 1.8±0.2-fold, respectively, when compared to the wild-type plants grown under the fixed light regime (Fig. 5f). We confirmed that the increases in biomass were not the consequence of alterations in photosynthesis per se42: CO2 assimilation under saturating light (600 μmol m-2s-1) was unaffected in any of the transgenic lines across the physiological range of internal CO2 concentrations. Thus, complementing with GORK mutated to affect its gating, enhanced stomatal dynamics to improve water use efficiency and enhance carbon assimilation. EXAMPLE VII: GORK mutations within the C-linker domain significantly alter voltage- dependent gating properties in GORK Kv channels We carried out alanine-scanning mutagenesis of the first 23 amino acid residues of the GORK N-terminus and the 39 C-linker hairpin residues. In both the C-linker and N-terminus domain we identified that substitutions of single residues within these domains generated significant changes in voltage-gated potassium channel kinetics. Alanine scanning identified that the Arginine residues at position 3, 5, 6 and 7 within the N-terminus are particularly critical determinants of channel properties (Figure 9). The alanine substitution effected all of the key channel parameters. Figure 10 shows that the effects observed in the single residue mutations within the N-terminus are not additive. Given the importance of the single residues within this first portion of the N-terminus, we decided to compare the effect of deleting different sized portions of the N-terminus. As shown in Figure 8, deleting residues 2 to 12 of the N-terminus surprisingly produced a greater effect on voltage-dependent gating properties than deleting residues 2 to 50. Deletion of the first 12 residues created a largely equivalent effect to deleting the first 23 residues of GORK. That the first portion of the N-terminus confers the key residues for GORK gating properties, supporting our theory that these residues act as an important pore ‘ball’ and is a key determinant of gating properties of GORK. Alanine scanning identified that the C-linker contains critical residues for voltage-gated potassium channel sensitivity and conductance. In particular, the negatively charged residues at positions 317 and 321 of AtGORK (i.e. within the C-linker of GORK) 14051746-1 drastically altered the channel’s sensitivity to K+ and caused severe deactivation delays. With severe deactivation delays, the channel pore is open significantly longer and K+ flux is significantly greater. The drastic effects of these few mutations are shown in Figures 14 to 18. Unlike the point mutations within the N-terminus, the effect of the point mutations within the C-linker are additive (Figure 15 and 16). As described above, the scale of the change caused by these point mutations is highly surprising since there was no indication that single residues within the C-linker of GORK generally would be such a key determinant. When the effect of a partial and whole N-terminal deletion and the C-linker E317A:D321A mutation were compared, we found that the C-linker mutation had a greater effect on channel kinetics (Figure 12). This was highly surprising because the C-linker mutation was comparatively much smaller, and the significance of the C-linker on gating and channel conductance of voltage-gated potassium channels was previously unknown. EXAMPLE VIII: Methods The effect of these critical regions on channel kinetics was measured using in vivo voltage clamp recordings within guard cells using standard protocols. Briefly, mutant GORK channels were introduced into the gork null mutant (GORK-myc) background by Agrobacterium co-cultivation that yields transiently transformed guard cells. We used bicistronic vectors with separate xFP markers to validate expression on a cell-by-cell basis. This approach circumvents problems with xFP tagging of some channels. Mutants were compared with wild-type plants and wild-type GORK transformants to determine effects on K+ inhibition of gating. Plant growth, transformation and whole-plant physiology Tobacco (Nicotiana tabacum) were grown and leaves transformed by Agrobacterium infiltration. Arabidopsis (Arabidopsis thaliana) wild-type (Col0), the gork null mutant and its complementation lines were sterilized and grown at 22:18oC and 9:15 h light:dark cycles. The characteristics of the gork mutant background and its phenotype are described elsewhere. Gas exchange measurements and growth experiments were carried out using LICOR 6800 gas exchange systems (Lincoln, USA) as described previously. Soil water content 14051746-1 was monitored using a ML3 moisture sensor (DeltaT Devices, Cambridge UK) and plants watered at 1- to 3-d intervals to maintain 8±4% soil water content. Confocal microscopy Transformed tobacco and Arabidopsis leaves were imaged on a Leica SP8 SMD confocal microscope equipped with 20x / 0.85 NA dry and 40x / 1.3 NA oil lenses and hybrid GaAs detectors (Leica, Wetzlar, Germany). Fluorescence was excited with the 488 nm laser line and emitted light was collected across 495-550 nm for GFP. Chloroplast autofluorescence was collected across 630-690 nm. Laser intensities and detector gains were standardized between sets of experiments for quantitative analysis. Oocyte and guard cell electrophysiology Electrical recordings of K+channels expressed in Xenopus oocytes were carried out using a standard protocols and a two-electrode voltage clamp. cRNAs were injected at 1 ^g / oocyte. Recordings were carried out 48-72 h after injection and oocytes were collected and analyzed for protein expression. Oocytes were superfused with 1, 10, 30 and 60 mM K+in modified ND96 buffer with 1.8 mM MgCl2, 1.8 mM CaCl2 and 10 mM HEPES-NaOH, pH 7.2 adjusted for osmotic balance31,66. All recordings were carried out using Henry’s EP suite (v.3.5.5.5, Y-Science, Glasgow, UK). Currents from intact guard cells in epidermal peels were recorded using double-barrelled microelectrodes and Henry’s EP suite. Guard cells were superfused with 1, 10, and 30 mM KCl in 5 mM Ca2+-MES, pH 6.1 ([Ca2+] = 1 mM). Voltage was clamped in cycles from holding voltages at least -50 mV from EKwith positive-going steps for outward-rectifying currents. Voltage was clamped in cycles from a holding voltage of -100 mV with negative- going steps for inward-rectifying currents. Currents were analyzed using Henry’s EP suite (Y-Science, Glasgow) and SigmaPlot 11.2 (Systat Software, Inc., USA) as described previously, and steady-state currents were fitted by joint, non-linear least- squares using the Boltzmann function of Eqn [1]. OnGuard modelling and statistics Quantitative modelling using OnGuard3. All other results are reported as means ±SE of n independent experiments. Significance was determined by Analysis of Variance (ANOVA), as appropriate with post-hoc analysis (Student-Newman-Keuls, Holm-Sidek and Tukey), and is indicated at P<0.05 unless otherwise stated. 14051746-1 SEQUENCE LISTING SEQ ID NO: 1 A.thaliana GORK CAC17380.1. C-linker domain in bold. MGRLRRRQEIIDHEEEESNDDVSSRRGKLSLAETFRWLDSSEHRRIETDGHNDYKYIIHPKNRWYKAWEMFI LVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQSYRTVYKPTRIAFRYLKSHFLMD FIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRINYLFTRILKLLFVEVYCTHTAACIFYYLA TTLPPEQEGYTWIGSLKLGDYSYENFREIDLWKRYTTALYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFD MVLGAYLIGNVTALIVKGSNTERFRDKMNDLISFMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIP ASIRAKIAQLLYLPYIKKVPLFKGCSTEFINQIVIRLHEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGS EESVTLLGPHTSFGDISIICNISQPFTVRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLES DIVIHIGKQEAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVNL KDKFGHTPLFEAVKAGQEGVIGLLVKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMNPNSEDYDHRTP LHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDVKNAQSSIYPSSLRELQEERIE RRKCTVFPFHPQEAKEERSRKHGVVVWVPSNLEKLIVTAAKELGLSDGASFVLLSEDQGRITDIDMISDGHKL YMISDTTDQT SEQ ID NO: 2 >A.thaliana GORK mRNA ATGGGACGTCTCCGGAGACGGCAAGAGATAATAGATCATGAAGAAGAGGAATCAAACGACGACGTTT CATCAAGAAGAGGAAAACTCAGTTTAGCCGAGACGTTTCGGTGGCTTGATTCATCAGAGCATCGGAGA ATTGAAACCGATGGTCATAATGATTATAAATACATCATTCATCCCAAAAACAGGTGGTACAAGGCATGG GAAATGTTTATATTGGTGTGGGCAATATACTCCTCATTGTTCACTCCCATGGAGTTTGGTTTCTTCCGCG GTCTGCCTGAGAGACTCTTTGTACTTGACATTGTTGGTCAGATCGCGTTCTTGGTCGATATTGTTCTTCA GTTCTTTGTTGCCTATCGCGATACTCAGTCCTACCGGACTGTCTACAAACCAACACGTATTGCTTTCCGG TACTTGAAGTCGCATTTTCTCATGGATTTCATCGGTTGCTTCCCTTGGGATCTTATTTATAAGGCATCAG GGAAACATGAGTTGGTGAGGTACTTGTTGTGGATAAGGCTATTTCGGGTTCGCAAAGTGGTTGAGTTT TTCCAAAGGCTTGAGAAAGACACAAGAATCAACTATCTATTCACTAGAATCTTAAAGCTCTTGTTCGTTG AAGTTTATTGTACTCACACTGCTGCTTGTATCTTCTATTACTTGGCCACCACTCTTCCTCCAGAACAAGAA GGGTACACGTGGATCGGTAGCTTGAAGCTAGGAGACTATAGCTACGAGAATTTCCGAGAAATCGATCT ATGGAAACGTTATACTACTGCTCTATACTTCGCCATTGTCACTATGGCAACTGTCGGTTATGGAGACATT CACGCGGTGAATCTGAGGGAAATGATATTTGTAATGATATATGTTTCATTTGATATGGTTCTCGGTGCTT ACCTTATTGGTAACGTCACTGCCTTGATTGTGAAAGGTTCAAACACAGAGAGGTTCAGAGATAAAATGA ATGATCTCATAAGTTTCATGAACCGCAAAAAACTCGGGAGAGACCTTCGTAGCCAGATAACTGGTCATG TTAGATTGCAGTACGACAGTCACTACACCGACACTGTCATGCTTCAGGACATCCCAGCATCAATCCGCG CCAAGATTGCGCAATTATTGTATCTGCCTTACATCAAAAAAGTTCCTCTCTTCAAAGGCTGCTCCACAGA GTTTATCAATCAAATAGTTATAAGGCTCCATGAAGAGTATTTTCTTCCAGGAGAAGTAATAACAGAGCA AGGAAACGTCGTGGATCATTTGTATTTCGTCTGTGAAGGCTTACTGGAGGCTCTTGTTACAAAAACAGA TGGATCAGAAGAGAGTGTGACGTTACTTGGGCCTCACACTTCTTTTGGAGACATCTCCATCATTTGCAA CATTTCTCAACCTTTCACTGTTAGGGTTTGTGAGCTATGCCATCTTTTACGACTCGATAAACAGTCTTTCT CAAACATCCTCGAGATTTATTTTCACGACGGACGCACAATCTTGAACAATATTATGGAGGAGAAGGAAT CAAATGATAGGATAAAGAAGCTAGAATCTGACATAGTGATTCACATTGGGAAACAAGAAGCAGAACTT GCATTGAAAGTAAACAGTGCAGCTTTCCAAGGAGATTTTTACCAGCTTAAGAGCTTAATCCGATCTGGA GCCGATCCTAACAAAACCGATTACGATGGAAGATCACCGCTTCATCTTGCAGCATGTAGAGGCTATGAA GACATTACATTATTCCTTATTCAGGAAGGTGTTGATGTCAATCTAAAAGATAAGTTCGGACACACACCAT TGTTTGAGGCTGTGAAAGCAGGACAAGAAGGAGTGATTGGTTTGCTTGTCAAAGAAGGAGCCTCCTTT 14051746-1 AATTTAGAAGATTCAGGAAACTTCCTTTGCACGACAGTTGCTAAAGGCGACTCTGATTTTCTCAAGAGA TTGCTTTCAAGCGGTATGAACCCAAACAGTGAAGATTATGATCACAGAACGCCGCTTCATGTCGCGGCT TCTGAAGGGTTATTCTTGATGGCTAAAATGTTGGTTGAAGCTGGAGCAAGCGTTATTTCTAAAGACCGA TGGGGGAATTCTCCGCTTGATGAAGCCCGATTGTGCGGAAACAAGAAACTGATTAAGTTACTCGAAGA TGTGAAAAATGCTCAGTCGTCTATCTACCCGTCAAGCTTGCGTGAATTACAAGAGGAGAGAATTGAGA GACGGAAATGCACGGTGTTTCCATTCCACCCGCAAGAGGCGAAAGAAGAGCGTAGTAGAAAGCACGG AGTTGTGGTTTGGGTCCCAAGCAATCTCGAGAAACTCATAGTAACCGCTGCGAAAGAGCTAGGGCTAT CGGATGGAGCCTCATTTGTACTATTATCAGAAGACCAAGGTCGTATCACAGACATTGATATGATTAGTG ATGGACACAAATTGTATATGATCAGTGATACTACTGATCAAACATAA SEQ ID NO: 3 >Brassica napus GORK XP_013656069.1 MGCLRRRQESIAEEDDINDDVSRRRGGFSLAESFRWLDSPEHLKDDSDGPNEYPWIIKPSISRWYKAWELFI LVWAIYSSLFTPMEFGFFRGLPENLFILDIVGQIAFLVDIVLQFFVAFQDKHNYRIDSKPTHIALRYLKSHFFLDL VSCFPWDLIYKASGKHEVVRYILWIRLFRVRKVIEFFQRLEKDTRINYLFTRILKLIFVEVYCTHTAACIFYYLATT LPAENEGYTWIGSLKLGDYSYENFRKIDIWKRYTTSLYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVL GAYLIGNITALIVKGSNTERFRDKMNDLASFMNRKKLRGDIRSQITHHVRLQYDSKFTNTVMLQDIPASIRAK IAQLLYTPYIEKIPLFKGCSSEFINQIVVRLHEEYFFPGEVITEQGNVVDHLYFVCEGSLEALETKTDGTEDLVELL EPHTSFGDISIICNISQPFTIRVRSLCHLLRLDKQSFSNILEIYFHDGRKILNNLMEGKESNERIKKLESDIMIHIGK QEAELALKVNSAAFQGDIYQLKSLVRSGADPNKTDYDGRAPLHLAASRGYEDITLFLIQEGVDINQKDKFGN TPLLEAVKAGQDRVIDLLVKEGASFDLEDAGNFLCTVVVKGDSDFLKRLLSSGMDPNTEDYDHRTPLHVAAS EGLFLMAKMLVEAGASVVAKDRWGNSPLDEARMCGNKKLIKLLEDADTAQPYIRPSSFHEPQDEKFERRKC TVFPFHPHEEPSRKHGVMVWLPRDLQKLVETAAQELGISNEVSFVILAEEGGRITDIDMISDGQKLYLISDST DQST SEQ ID NO: 4 >Brassica napus GORK mRNA ATGGGGTGTCTCCGGCGACGGCAAGAGAGTATAGCCGAGGAAGATGATATAAACGACGACGTTTCAA GGAGAAGAGGTGGGTTCAGCTTGGCCGAGTCGTTCCGGTGGCTTGATTCCCCTGAGCATCTGAAAGAT GATTCCGATGGCCCTAACGAATACCCTTGGATCATTAAGCCCTCAATTAGGTGGTACAAGGCATGGGA GTTATTCATATTGGTCTGGGCAATATACTCGTCTTTGTTCACTCCCATGGAGTTTGGTTTCTTCCGCGGTC TACCCGAAAACCTCTTCATACTCGACATTGTTGGTCAGATCGCATTTTTGGTCGATATTGTTCTACAGTTT TTTGTCGCCTTCCAAGATAAGCATAACTACCGAATTGACAGCAAACCAACACATATTGCTCTCCGGTACT TGAAATCGCATTTTTTCTTGGATTTGGTCAGTTGCTTCCCATGGGATCTCATCTATAAGGCTTCAGGGAA ACATGAGGTGGTGAGGTACATATTGTGGATAAGGCTGTTTCGTGTGCGCAAAGTGATTGAGTTCTTCC AAAGGCTTGAGAAAGACACGAGAATCAACTATCTCTTCACCAGAATCTTGAAGCTCATTTTCGTTGAGG TTTACTGTACTCACACTGCTGCATGCATCTTCTATTACTTGGCCACCACTCTTCCTGCTGAGAACGAAGG TTATACTTGGATCGGTAGCCTGAAGTTAGGAGACTATAGCTACGAGAATTTCCGAAAGATCGACATCTG GAAACGTTACACCACATCTCTCTACTTCGCCATTGTCACTATGGCTACTGTCGGTTATGGAGACATACAT GCCGTAAATTTAAGGGAAATGATATTTGTAATGATATATGTTTCGTTCGATATGGTTCTTGGTGCGTACC TTATTGGTAACATCACTGCCTTGATTGTGAAAGGATCAAACACAGAGAGATTTAGAGATAAAATGAATG ATCTGGCAAGTTTCATGAACCGAAAAAAACTTAGGGGAGACATTCGTAGCCAGATAACTCATCACGTTA GATTGCAGTACGACAGTAAATTCACCAACACTGTCATGCTTCAAGACATCCCAGCCTCTATCCGCGCCA AGATTGCGCAGTTATTATACACGCCTTACATTGAGAAAATCCCTCTGTTCAAGGGCTGCTCATCAGAGTT TATTAACCAGATAGTTGTAAGGCTCCATGAAGAGTATTTTTTTCCAGGAGAAGTAATCACAGAGCAAGG AAACGTCGTTGATCATTTGTATTTCGTCTGTGAAGGCTCACTGGAGGCTCTTGAAACAAAAACAGATGG AACAGAAGACCTTGTGGAGTTGCTTGAGCCTCACACTTCTTTTGGTGATATATCCATCATCTGCAACATC TCTCAACCTTTCACTATTAGAGTTCGTTCATTGTGCCATCTTTTACGCCTCGATAAACAGTCTTTCTCCAA 14051746-1 CATCCTCGAGATTTATTTTCATGATGGACGCAAAATCCTAAACAATCTTATGGAGGGTAAAGAATCAAA TGAGAGGATAAAGAAGCTCGAATCTGACATTATGATTCACATTGGGAAACAAGAAGCAGAACTTGCAT TGAAGGTAAACAGTGCAGCTTTCCAAGGAGATATCTACCAGCTTAAAAGCTTAGTCCGCTCTGGCGCCG ATCCTAACAAAACAGATTACGATGGAAGAGCACCGCTTCATCTTGCAGCGTCTAGGGGATACGAAGAC ATTACATTGTTTCTTATTCAAGAAGGCGTCGATATAAATCAAAAAGATAAATTTGGCAATACACCATTGT TAGAGGCTGTAAAAGCAGGGCAAGACAGAGTGATCGATTTGCTTGTCAAAGAAGGAGCTTCCTTTGAT TTAGAAGATGCTGGAAACTTTCTCTGCACGGTAGTTGTGAAAGGCGACTCTGATTTTCTTAAGAGATTG CTCTCAAGCGGTATGGACCCAAACACCGAAGATTATGATCATAGAACACCGCTTCATGTCGCTGCTTCA GAAGGCTTATTCTTGATGGCTAAGATGCTTGTTGAAGCTGGAGCTAGCGTTGTCGCTAAAGACCGGTG GGGAAACTCTCCGCTTGATGAAGCTCGAATGTGTGGAAACAAGAAATTGATTAAGTTACTTGAAGACG CGGATACAGCTCAGCCTTATATACGCCCGTCAAGCTTTCATGAACCACAAGATGAGAAATTTGAGAGAC GGAAATGCACAGTGTTTCCATTCCACCCACATGAGGAGCCGAGTAGAAAGCATGGAGTTATGGTTTGG CTTCCGCGTGACCTCCAGAAACTTGTGGAAACAGCTGCGCAAGAGCTCGGGATATCTAATGAAGTCTCC TTTGTAATATTGGCCGAGGAAGGAGGTCGAATCACAGACATTGATATGATCAGTGATGGACAGAAACT GTATTTGATCAGTGATAGTACTGATCAATCAACCTGA SEQ ID NO: 5 >Raphanus sativus (Radish) GORK XP_018433301.1 MGCLRRPQESIAEEDDTNDDVSMRRGRFSLAESFRWLDSPEHLKNDSDCPNEHPWIINPSNRWYKAWELF ILLWAIYSSLFTPMEFGFFRGLPENLFVLDIIGQIAFLVDIVIQFFVAFQDKHTYRTDDKPTHIALRYMKSHFFL DLVSCFPWDLIYKASGKNEVVRYILWIRLFRVRKVIEFFQRLEKDTRINYLFTRILKLIFVEVYCTHTAACIFYYLA TTLPAENEGYTWIGSLKLGDYSYENFRKIDIWKRYTTSLYFAIVTMATVGYGDIHAVNLREMIFVMIYVSLDM VLGAYLIGNITALIVKGSNTERFRDKMNDLASFMNRKKLRGDIRSQITHHVRLQYDSKFTNTVMLQDIPASIR AKIAQLLYTPYIEKIPLFKGCSSEFINQIVIRLHEEYFFPGEVITEQGNVVDHLYFVCEGSLEALATKTDGTEELVA LLEPHTSFGDISIICNISQPFTVRVRSLCHLLRLDKQSFSNILEIYFHDGRKILNNLMEGKESNERIKELEPDVMIH IGKQEAELALKVNSAAFQGDIYQLKRLVRSGADPNKTDYDGRAPLHLAASRGYEDITLFLIQEGVDINQKDKF GNTPLLEAVKAGQDRVIHVLVKEGASFDLEDAGNFLCTVVLKGDSDFLRRLLSSGMDPNTEDYDHRTPLHV AASEGLFLMAKMLVEAGARVVAKDRWGNSPLDEARICGNKKLIKLLENARTAQPSICPSSSHELQDEKFKRR KCTVFPFHPHEEPNRKHGVMVWLPRDLQKLVETAAQELRLSNEASFVILSEEGGRITDVDMISDGQKLYLIS DSTDQSA SEQ ID NO: 6 >Raphanus sativus (Radish) GORK mRNA ATGGGGTGTCTCCGGCGACCGCAAGAGAGTATAGCCGAGGAAGACGATACAAACGACGACGTTTCAA TGAGAAGAGGTAGATTCAGCTTGGCCGAGTCGTTCCGGTGGCTTGATTCCCCCGAGCATCTGAAAAAT GATTCCGATTGCCCTAACGAACACCCTTGGATCATTAATCCCTCAAACAGGTGGTACAAGGCATGGGAG TTATTCATATTGTTATGGGCAATATATTCGTCTTTGTTCACTCCCATGGAGTTTGGTTTCTTCCGCGGTTT ACCCGAAAACCTCTTCGTACTCGACATTATTGGTCAGATTGCATTTTTGGTCGATATTGTTATACAGTTTT TCGTTGCCTTCCAAGATAAACATACCTACCGGACTGACGACAAACCAACACATATTGCTCTCCGGTACAT GAAATCGCATTTTTTCTTGGATTTGGTCAGTTGCTTCCCATGGGATCTCATCTATAAGGCGTCAGGGAAA AACGAGGTGGTGAGGTACATATTGTGGATAAGGCTGTTTCGTGTGCGCAAAGTGATAGAGTTCTTCCA AAGGCTTGAGAAAGACACGAGAATCAACTATCTGTTCACCAGAATCTTGAAGCTCATTTTTGTTGAGGT TTATTGTACTCACACTGCTGCATGCATCTTCTATTACTTGGCCACCACTCTTCCTGCCGAGAACGAAGGT TACACTTGGATCGGTAGCCTGAAGTTAGGAGACTATAGCTACGAGAATTTCCGAAAGATCGACATTTG GAAACGTTATACCACATCTCTCTACTTCGCCATTGTCACTATGGCTACTGTCGGTTATGGAGACATACAC GCGGTAAATTTAAGGGAAATGATATTCGTAATGATATATGTTTCACTCGATATGGTTCTGGGTGCGTAC CTTATTGGTAACATCACTGCCTTGATAGTGAAAGGATCAAACACAGAGAGATTTAGAGATAAAATGAAT GATCTGGCAAGTTTCATGAACCGAAAAAAACTACGGGGAGACATTCGAAGCCAGATAACTCATCACGT 14051746-1 TAGATTGCAATACGACAGTAAATTCACCAACACTGTCATGCTTCAAGACATCCCAGCCTCTATCCGCGCC AAGATTGCCCAATTATTATACACGCCTTACATTGAGAAAATCCCTCTGTTCAAGGGCTGTTCATCAGAGT TTATTAACCAGATAGTTATAAGGCTCCACGAAGAGTATTTTTTTCCGGGAGAAGTAATCACAGAGCAAG GAAACGTTGTTGATCATTTGTATTTCGTCTGTGAAGGCTCACTGGAGGCTCTTGCTACAAAAACAGATG GAACAGAAGAGCTTGTGGCGTTGCTTGAGCCTCACACTTCTTTTGGTGATATCTCCATCATTTGCAACAT CTCTCAACCTTTCACTGTTAGAGTTCGTTCATTATGCCATCTTTTACGCCTGGATAAACAGTCTTTCTCCA ACATCCTCGAGATTTATTTTCATGATGGACGCAAAATTCTAAACAATCTTATGGAGGGTAAGGAATCAA ATGAGAGGATAAAGGAGCTAGAACCTGATGTTATGATTCACATTGGGAAACAAGAAGCAGAACTTGCA CTGAAGGTAAACAGTGCAGCTTTCCAAGGAGATATCTACCAGCTTAAAAGATTAGTCCGCTCTGGAGCC GATCCTAACAAAACAGATTACGATGGAAGAGCACCGCTTCATCTTGCAGCGTCTAGGGGATACGAAGA CATTACATTGTTTCTTATTCAAGAAGGCGTCGATATAAATCAAAAAGATAAATTTGGGAATACACCATTG TTAGAGGCTGTAAAAGCAGGGCAAGACAGAGTGATCCATGTGCTTGTCAAAGAAGGAGCTTCCTTTGA TTTAGAAGATGCTGGAAACTTTCTTTGCACGGTCGTTCTGAAAGGCGACTCTGATTTTCTTAGGAGATT GCTCTCAAGCGGTATGGACCCAAACACCGAAGATTATGATCATAGAACACCACTTCATGTCGCTGCTTC TGAAGGATTATTCTTGATGGCTAAGATGCTTGTTGAAGCTGGAGCTAGAGTTGTCGCTAAAGACAGGT GGGGAAACTCTCCTCTTGATGAAGCTCGAATATGTGGAAACAAGAAATTGATTAAGTTACTTGAAAAC GCGAGAACAGCTCAGCCTTCTATATGCCCGTCAAGCTCTCATGAACTACAAGATGAGAAATTTAAGAGA CGGAAATGCACAGTGTTTCCATTCCACCCACACGAGGAGCCTAATAGAAAGCATGGAGTCATGGTGTG GCTTCCGCGTGATCTACAGAAACTTGTGGAAACAGCTGCGCAAGAGCTCAGGCTATCTAATGAAGCCTC CTTTGTAATATTGTCAGAGGAAGGAGGTCGAATCACAGACGTTGATATGATCAGTGATGGACAGAAAC TGTATTTGATCAGTGATAGTACTGATCAATCAGCGTGA SEQ ID NO: 7 >Elaeis guineensis (Oil palm) KOR1 XP_010905454.2 MSPRAKNGSPEIEYELEEPIASSRGIRLFLLTSEFALGPLRRRRATSQEKLLERFVIEPDNRWYQLWTRFILVWA LYSSFFTPIEFGFFRGLPNNLFWLDFAGQVAFLVDIFVQFLVAYRDSHTYRMIYEPTSIAVRYAKSSFVFDLLGC FPWDAIYRACGRKEEVRYLLWIRLTRVRKVTDFFQKMEKDIRINYLFTRIVKLIVVELYCTHTAACIFYYLATTLP ASMEGYTWIGSLKLGDYSYSHFRDMDIAKRYITSLYFAIVTMATVGYGDIHAVNPREMVFIMIYVSFDMILG AYLIGNMTALIVKGSKTERFRDRMKELIKYMNRNKLGKDIRDQIKGHVRLQYESSYTEASVLQDIPVSIRAKIS QTLYKPYIENVPLFKGCSAEFIHQIIIKLQEEFFLPGEVILEQGNAVDQLYFVCHGKLEGVGIGEDGPLELEPNSS FGEIAILCNIPQPYTVRVCELCRLLRIDKQIFTNILQIYFVDGRKILSNLLEGNDSIQIKQLEGDIIFHIGKQEAELA LRVNNAAFYGDLHYLKGLIQAGADPNKTDYDGRSPLHLAAAKGHEDITLFLIQEGVNINLSDNFGNTPLFEA VKVGHDRVASLLFSRGAQLNLKDAGSHLCTAAAKGDSDFIRRALSYGVDPNSKDYDHRTALHIAASEGLYFI AKLLLEAGASVFAMDRWGATPLDEGRKSGNQSLMLLLEGAKSDELSKFPEHAREVQDKMHPRRCTVFPFH PWDPKEARREGVVLWIPCTIEELIRSSREQLKSSGSCILSEDGGRILDVDMISDGQKLYLVADQETTAHNNQH T SEQ ID NO: 8 >Elaeis guineensis (Oil palm) KOR1 mRNA ATGGGTCCCCGGAGATCGAGTACGAGTTGGAGGAGCCGATTGCGTCGTCGCGGGGGATCCGCCTTTTC CTGCTCACCTCCGAATTCGCCCTCGGCCCCCTCCGCCGCCGCCGGGCGACCAGCCAGGAGAAGCTTCTC GAGCGCTTCGTCATCGAACCCGATAACCGGTGGTACCAGCTGTGGACGAGGTTTATACTGGTATGGGC ATTGTACTCGTCCTTCTTCACGCCGATAGAGTTCGGCTTCTTCAGGGGGCTCCCGAACAACCTCTTCTGG CTCGATTTCGCCGGCCAGGTGGCCTTCCTCGTCGACATCTTCGTCCAGTTCCTCGTCGCCTACCGTGACT CTCACACCTACCGCATGATCTACGAGCCCACCTCCATTGCTGTCCGGTACGCGAAGTCGAGCTTCGTCTT CGACTTACTTGGCTGCTTTCCTTGGGATGCTATCTATAGGGCATGCGGACGTAAAGAGGAAGTGAGGT ACCTTTTATGGATTCGATTAACTCGGGTGCGCAAAGTCACAGATTTTTTTCAGAAGATGGAGAAAGATA TCCGCATCAACTACTTGTTTACAAGAATTGTTAAACTCATAGTTGTGGAGCTCTACTGCACGCATACAGC 14051746-1 TGCCTGTATATTTTACTATCTTGCAACAACTTTGCCAGCATCCATGGAAGGCTATACATGGATAGGGAG CTTAAAGTTGGGTGATTATAGCTATTCGCACTTCAGGGATATGGATATCGCAAAGCGTTACATAACATC GTTATATTTTGCCATTGTCACAATGGCAACTGTTGGTTATGGAGACATACATGCAGTTAATCCCAGGGA GATGGTATTCATCATGATTTATGTTTCTTTTGATATGATTCTGGGAGCTTACCTTATTGGCAACATGACT GCATTGATTGTGAAAGGATCAAAGACAGAAAGGTTTAGGGACAGAATGAAAGAATTAATTAAATACAT GAACAGAAACAAACTTGGAAAGGATATTCGTGACCAGATCAAAGGACATGTACGCTTACAATATGAAA GCAGCTACACAGAGGCTTCAGTTCTTCAGGATATCCCAGTTTCAATTCGTGCTAAGATATCACAGACACT ATACAAACCGTATATCGAAAATGTTCCCCTGTTTAAGGGATGCTCAGCCGAATTCATTCACCAGATTATT ATCAAGCTGCAGGAAGAGTTTTTCCTTCCAGGGGAGGTGATATTGGAACAGGGAAATGCAGTAGATCA GCTATATTTTGTCTGCCATGGTAAGCTGGAAGGAGTAGGAATTGGTGAAGATGGACCTTTGGAACTGG AGCCCAACAGTTCCTTTGGAGAAATTGCGATTCTGTGCAACATTCCTCAGCCTTACACTGTTCGTGTTTG TGAATTGTGTAGACTTTTGCGAATTGATAAACAAATCTTCACAAATATTCTACAAATTTACTTTGTTGATG GTCGGAAAATTTTGAGCAACCTTCTAGAGGGTAATGATTCCATTCAAATTAAGCAACTAGAAGGTGATA TTATATTCCATATCGGTAAGCAAGAAGCCGAGCTTGCTTTAAGAGTAAACAATGCTGCTTTCTATGGAG ATCTCCATTACCTTAAAGGTTTGATCCAAGCAGGAGCAGATCCTAATAAGACTGATTATGATGGACGCT CACCTTTGCATCTCGCAGCAGCAAAAGGGCATGAAGATATCACTCTATTTCTCATTCAAGAAGGCGTGA ACATTAACCTTTCTGACAACTTTGGAAATACACCCTTGTTTGAGGCAGTCAAGGTTGGACATGATCGAG TGGCTTCTTTACTCTTTAGTAGAGGTGCACAATTAAATCTTAAAGATGCTGGTAGCCACCTTTGTACAGC TGCTGCAAAGGGGGATTCAGATTTTATTAGAAGAGCTTTATCTTACGGTGTTGATCCAAACTCAAAGGA CTACGATCACCGCACAGCGCTGCATATAGCTGCTTCTGAGGGATTATATTTTATAGCAAAGTTACTTTTA GAGGCTGGGGCAAGTGTTTTTGCTATGGACAGATGGGGAGCTACACCATTGGATGAAGGACGAAAGA GTGGAAACCAATCCTTGATGCTGCTGTTAGAAGGTGCAAAGTCTGACGAGCTGTCCAAGTTTCCTGAAC ATGCTCGGGAAGTTCAAGATAAAATGCATCCAAGGAGGTGCACAGTGTTTCCTTTTCACCCGTGGGATC CGAAAGAAGCAAGAAGAGAGGGAGTCGTGCTATGGATCCCATGCACCATAGAGGAGCTCATTAGATC CTCTAGAGAGCAGCTAAAGTCTTCAGGTTCATGCATACTATCAGAAGATGGGGGCAGGATTCTTGATGT AGATATGATATCTGATGGCCAGAAATTATATCTAGTTGCAGATCAAGAAACAACTGCACATAATAACCA GCATACTTGA SEQ ID NO: 9 > O.sativa KOR1 (rice)XP_015644419.1 MGRGIGSKRRVEDDDGENMPGRKKKEEEEEEEDDDGEEEYEVDVVRDRIGSSRGSRLALFGSDLRLGRFRP RRRRVAPVDGDDGIFQDFVIDPDNKWYRLWTRFILVWAVYSSFFTPLEFGFFRGLPRNLFFLDIAGQIAFLIDI VLRFFVAYRDPDTYRMVHNPTSIALRYCKSSFIFDLLGCFPWDAIYKACGSKEEVRYLLWIRLTRAMKVTEFFR SMEKDIRINYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGYTWIGSLQLGDYSYSHFREIDLTKRYMTSL YFAIVTMATVGYGDIHAVNVREMIFIMIYVSFDMILGAYLIGNMTALIVKGSRTERFRDKMKEVIRYMNRNK LGKDIREQIKGHLRLQYESSYTEASVLQDIPVSIRAKISQTLYKPYIESIPLFKGCSAEFIQQIVIRLQEEFFLPGEVI LEQGSAVDQLYFVCHGALEGVGIGEDGQEETILMLEPESSFGEIAVLCNIPQPFTVRVCELCRLLRLDKQSFTN ILEIFFVDGRRILSNLSESSEYGSRIKQLESDITFHIGKQEAELTLRVNNAAFYGDMHQLKSLIRAGADPKNTDY DGRSPLHLAACKGFEDVVQFLLHEGVDIDLSDKFGNTPLLEAVKQGHDRVATLLFSKGAKLSLENAGSHLCT AVARGDTDFVRRALAYGGDPNARDYDHRAPLHIAAAEGLYLMAKLLVDAGASVFATDRWGTTPLDEGRR CGSRTMVQLLEAAKSGELSRYPERGEEVRDKMHPRRCSVFPHHPWDGGERRREGVVVWIPHTIEGLVSSA QEKLGLAGSGEGLRLLGEDGARVLDVDMVHDGQKLYLVVGGGGDDGGTEARQ SEQ ID NO: 10 > O.sativa KOR1 (rice) ATGGGGAGGGGGATAGGGTCGAAGCGGAGGGTGGAGGACGACGACGGGGAGAATATGCCGGGGAG GAAGAAGAAGGAGGAGGAGGAGGAGGAGGAGGATGACGATGGGGAAGAGGAGTACGAGGTGGAC GTGGTGCGCGACCGGATCGGGTCGTCGCGGGGGAGCCGCCTGGCGCTGTTCGGCTCCGACCTCCGCCT 14051746-1 CGGCCGCTTCCGCCCGCGCCGCCGCCGCGTCGCCCCCGTCGACGGCGACGATGGCATCTTCCAGGACT TCGTCATCGACCCCGACAACAAGTGGTATCGGTTATGGACGAGGTTCATACTAGTGTGGGCAGTGTAC AGTTCCTTCTTCACGCCATTGGAATTTGGCTTCTTCAGGGGGCTCCCCAGGAACCTCTTCTTCCTAGACA TAGCTGGTCAGATCGCCTTCCTCATCGACATTGTTCTCAGGTTCTTCGTGGCCTACCGTGATCCTGACAC CTACCGCATGGTTCACAATCCCACCTCCATCGCTCTCCGATATTGTAAATCAAGCTTCATTTTTGATCTTC TTGGTTGTTTTCCGTGGGATGCTATCTATAAGGCTTGTGGAAGTAAAGAAGAAGTAAGATACCTATTGT GGATTCGGTTGACACGAGCTATGAAGGTGACAGAGTTCTTCAGGAGCATGGAAAAAGATATCCGTATA AATTACCTGTTTACTAGGATTGTGAAACTCATAGTTGTGGAACTCTACTGTACGCACACAGCAGCATGT ATCTTCTACTATCTTGCAACAACACTTCCTGAATCAATGGAAGGATATACATGGATAGGGAGCTTGCAG TTGGGAGACTATAGTTATTCTCATTTCAGGGAGATTGATCTTACCAAGCGTTATATGACATCGCTGTACT TTGCCATAGTCACCATGGCAACTGTTGGTTATGGTGACATTCATGCTGTGAATGTCAGGGAGATGATAT TCATCATGATTTATGTTTCCTTTGATATGATTCTTGGAGCCTACCTCATTGGTAACATGACTGCACTTATT GTCAAGGGCTCGAGAACCGAGCGATTCAGGGATAAGATGAAAGAAGTTATCAGGTACATGAACAGAA ACAAGCTTGGAAAGGACATAAGGGAACAGATTAAAGGACATTTGAGGTTGCAGTATGAAAGCAGCTA CACTGAAGCTTCTGTCCTTCAGGATATCCCAGTCTCAATTCGTGCGAAGATTTCACAAACACTGTATAAG CCATATATCGAAAGCATTCCACTGTTTAAAGGATGTTCAGCAGAATTCATTCAACAGATTGTGATCAGG CTGCAGGAAGAGTTCTTCCTACCCGGAGAGGTTATTTTGGAGCAGGGAAGTGCAGTTGATCAACTGTA CTTTGTCTGTCATGGGGCACTGGAAGGTGTTGGCATTGGTGAAGATGGTCAAGAAGAGACCATTCTAA TGCTAGAGCCTGAAAGTTCTTTTGGAGAAATCGCTGTTCTCTGCAATATCCCACAACCCTTCACCGTTCG TGTCTGCGAACTTTGTCGTCTTTTGCGGCTTGACAAGCAATCCTTCACAAACATCCTGGAGATCTTCTTC GTTGATGGAAGAAGAATTCTGAGCAACCTTTCTGAGAGTAGCGAATACGGCAGCCGGATCAAGCAGCT GGAATCCGACATCACGTTCCACATCGGGAAGCAAGAGGCAGAGCTGACGCTGCGAGTGAACAACGCT GCGTTCTACGGTGACATGCATCAGCTCAAGAGCCTGATCCGTGCAGGAGCCGATCCCAAGAACACCGA TTACGACGGGCGATCTCCTCTGCATCTTGCGGCTTGCAAAGGGTTCGAAGATGTCGTCCAGTTCCTCCT CCACGAAGGCGTCGACATCGATCTTTCCGACAAATTTGGCAACACGCCATTGCTGGAGGCGGTGAAGC AGGGGCACGACCGGGTGGCGACGCTGCTGTTCAGCAAGGGGGCGAAGCTGAGCCTGGAGAACGCCG GGAGCCACCTGTGCACGGCGGTGGCGAGGGGCGACACGGACTTCGTCCGGCGGGCGCTCGCCTACGG CGGCGACCCGAACGCGAGGGACTACGACCACCGCGCGCCGCTCCACATCGCCGCCGCCGAGGGCCTCT ACCTGATGGCGAAGCTGCTCGTCGACGCCGGCGCCAGCGTGTTCGCCACCGACCGGTGGGGCACGAC GCCGCTGGACGAAGGGCGCAGGTGCGGGAGCCGGACGATGGTGCAGCTGCTGGAGGCGGCCAAGTC CGGCGAGCTCTCCAGGTACCCGGAGCGCGGCGAGGAGGTGCGGGACAAGATGCACCCGCGGCGGTG CTCCGTGTTCCCGCACCACCCGTGGGACGGCGGCGAGCGGCGGCGGGAAGGGGTGGTGGTGTGGATC CCGCACACCATCGAGGGGCTCGTCAGCTCGGCGCAGGAGAAGCTCGGCCTCGCCGGCTCCGGCGAGG GGCTCCGGCTGCTCGGCGAGGACGGCGCCAGAGTGCTCGACGTCGACATGGTCCACGACGGGCAGAA GCTCTACCTCGTCGTCGGCGGCGGCGGCGATGACGGCGGCACGGAGGCAAGGCAGTGA SEQ ID NO: 11: > A.thaliana SKOR NM_111153.4 MGGSSGGGVSYRSGGESDVELEDYEVDDFRDGIVESRGNRFNPLTNFLGLDFAGGSGGKFTVINGIRDISRG SIVHPDNRWYKAWTMFILIWALYSSFFTPLEFGFFRGLPENLFILDIAGQIAFLVDIVLTFFVAYRDSRTYRMIY KRSSIALRYLKSTFIIDLLACMPWDIIYKAAGEKEEVRYLLLIRLYRVHRVILFFHKMEKDIRINYLFTRIVKLIFVEL YCTHTAACIFYYLATTLPASQEGYTWIGSLKLGDYSYSKFREIDLWTRYTTSMYFAVVTMATVGYGDIHAVN MREMIFAMVYISFDMILGAYLIGNMTALIVKGSKTERFRDKMADIMRYMNRNKLGRNIRGQITGHLRLQYE SSYTEAAVLQDIPVSIRAKIAQTLYLPYIEKVPLFRGCSSEFINQIVIRLHEEFFLPGEVIMEQGSVVDQLYFVCH GVLEEIGITKDGSEEIVAVLQPDHSFGEISILCNIPQPYTVRVAELCRILRLDKQSFMNILEIFFHDGRRILNNLLE GKESNVRIKQLESDITFHISKQEAELALKLNSAAFYGDLYQLKSLIRAGGDPNKTDYDGRSPLHLAASRGYEDIT LYLIQESVDVNIKDKLGSTPLLEAIKNGNDRVAALLVKEGATLNIENAGTFLCTVVAKGDSDFLKRLLSNGIDP 14051746-1 NSKDYDHRTPLHVAASEGFYVLAIQLVEASANVLAKDRWGNTPLDEALGCGNKMLIKLLEDAKNSQISSFPS GSKEPKDKVYKKKCTVYFSHPGDSKEKRRRGIVLWVPRSIEELIRTAKEQLNVPEASCVLSEDEAKIIDVDLISD GQKLYLAVET SEQ ID NO:12> A.thaliana SKOR mRNA ATGGGAGGTAGTAGCGGCGGCGGAGTTTCTTATCGTAGCGGCGGCGAATCAGACGTGGAATTAGAGG ATTACGAGGTTGATGATTTCAGAGATGGGATTGTAGAATCGCGAGGAAACAGATTCAATCCTCTCACCA ATTTCTTAGGGTTAGACTTCGCCGGCGGTAGCGGTGGAAAGTTCACCGTCATTAATGGAATCAGAGAT ATCTCCAGAGGCTCCATTGTTCATCCCGATAACCGGTGGTACAAGGCGTGGACGATGTTTATATTGATA TGGGCACTTTATTCTTCCTTCTTCACTCCATTGGAATTCGGATTCTTCAGGGGATTACCAGAGAATCTGTT CATCCTCGATATCGCTGGCCAAATCGCTTTCTTAGTAGATATTGTCTTGACATTCTTCGTTGCTTATCGTG ATAGCCGAACTTATAGAATGATCTATAAACGCAGCTCAATTGCTTTACGGTACTTAAAATCAACTTTTAT AATTGACTTACTTGCTTGCATGCCATGGGATATCATCTACAAGGCTGCAGGCGAAAAAGAAGAAGTGA GATACCTATTGTTGATAAGGCTATATCGAGTTCATAGAGTAATCCTGTTTTTCCACAAAATGGAGAAAG ATATAAGAATCAATTACCTTTTTACAAGAATCGTCAAGCTTATATTCGTCGAGCTTTATTGCACTCACACC GCAGCTTGTATCTTCTATTACTTGGCCACGACGCTTCCTGCTTCTCAAGAAGGGTACACTTGGATTGGAA GCTTGAAGTTAGGAGATTACAGTTACTCGAAGTTTAGAGAGATCGATCTCTGGACTCGATACACTACTT CTATGTACTTTGCAGTTGTTACTATGGCAACTGTTGGTTATGGAGATATACACGCGGTTAATATGCGGG AAATGATATTCGCGATGGTCTACATTTCATTCGATATGATTCTAGGAGCTTACTTGATTGGTAACATGAC AGCTTTGATTGTAAAAGGTTCGAAAACAGAGAGATTCCGGGATAAGATGGCTGATATCATGCGGTATA TGAACCGAAACAAACTCGGTAGGAACATCCGTGGTCAGATTACCGGACATTTGCGGTTGCAGTACGAA AGCAGCTACACTGAAGCAGCTGTTCTTCAAGACATTCCTGTCTCTATCCGTGCTAAGATTGCGCAAACTT TATACTTGCCGTATATTGAGAAAGTTCCTCTCTTTCGCGGATGCTCATCTGAATTCATTAACCAGATTGTT ATAAGACTTCATGAAGAGTTCTTTCTTCCTGGAGAAGTTATAATGGAGCAAGGAAGCGTCGTTGATCAG CTCTACTTTGTTTGTCACGGTGTATTGGAGGAGATAGGTATAACAAAGGATGGATCTGAAGAAATAGT GGCAGTTCTACAACCAGATCATTCTTTTGGAGAGATTTCAATCCTCTGCAATATTCCTCAGCCTTACACG GTTAGAGTTGCAGAGCTATGTCGGATTCTAAGGCTTGACAAGCAATCTTTCATGAACATACTCGAGATA TTTTTCCATGATGGACGGAGGATTCTCAACAATCTGCTTGAAGGGAAAGAATCTAATGTCCGGATTAAG CAACTAGAATCCGATATAACCTTTCATATCAGTAAACAAGAGGCAGAGCTAGCTCTGAAGTTGAATAGT GCGGCTTTCTACGGTGATCTTTATCAGCTTAAGAGTTTGATTCGAGCTGGAGGTGACCCGAATAAGACA GATTATGACGGAAGATCGCCTTTGCATCTTGCAGCCTCTAGAGGATATGAAGATATTACATTATATCTTA TACAAGAATCAGTTGATGTAAATATCAAAGATAAATTGGGGAGCACACCTTTACTAGAAGCAATCAAG AATGGGAATGATCGTGTTGCGGCGTTGCTTGTTAAAGAAGGAGCTACGTTGAACATAGAGAACGCAG GGACTTTCCTTTGCACCGTGGTTGCGAAAGGAGACAGCGATTTCTTGAAACGGCTTCTTAGTAACGGAA TTGATCCTAATTCCAAAGATTATGATCACAGAACACCTCTTCATGTAGCTGCCTCTGAAGGATTTTATGT CTTGGCGATCCAATTGGTAGAAGCAAGTGCTAATGTTCTTGCAAAAGACAGATGGGGAAACACACCTC TTGATGAAGCTTTGGGTTGTGGGAACAAGATGTTGATAAAGTTACTCGAAGACGCTAAGAATTCTCAA ATCTCTTCGTTTCCGAGTGGCTCCAAAGAGCCTAAAGATAAAGTCTATAAGAAGAAATGTACAGTGTAT TTTTCACATCCTGGTGATTCGAAAGAGAAAAGAAGGCGCGGGATTGTACTGTGGGTACCTCGAAGCAT CGAGGAGCTTATAAGAACAGCAAAGGAGCAGCTGAATGTTCCGGAGGCTTCTTGTGTATTATCTGAAG ATGAAGCCAAAATTATTGATGTAGATTTGATAAGTGATGGACAAAAACTGTATTTGGCTGTTGAAACAT AA SEQ ID NO: 13> Brassica napus SKOR X1_XP_013750920.1 MGGSSGGGVSYRSEVDSDVELEDYEVDDDFGEGIVESRGNRFNPLTNFLGLDFTGGNGGKFTVINGIRDISR GSVVHPDSGCYKAWTMFIVIWALYSSFFTPLEFGFFRGLPGNLFILDILGQIAFLVDIVLTFFVAYRDSRTYRM 14051746-1 VYRRSSIALRYLKSTFIIDFLSCMPWDIIYKVAGRKEEVRYLLLIRLYRVRRVILFFHKMEKDIRINYLFTRIVKLIFV ELYCTHTAACIFYYLATTLPASQEGYTWIGSLKLGDYSYAKFREIDLWTRYTTSMYFAVVTMATVGYGDIHAV NMREMIFAMAYISFDMILGAYLIGNMTALIVKGSKTERFRDKMADIMRYMNRNKLGRNIRGQITGHLRLQ YESSYTEAAVLQDIPVSIRAKIAQTLYLSYIEKVPLFRGCSSEFINQIVIRLHEEFFLPGEVIMEQGSVVDQLYFVC HGVLEEIGTAKDGSEEIVSLLQPDNSFGEISILCNIPQPYTVRVSELCRVLRLDKQSFMNILEIYFHDGRRILNNL LEGKESNGRIKQLESDITFHISKQEAELALKLNSAAFYGDLYQLKSLIRAGADPNKTDYDGRSPLHLAASRGYE DITLYLIQESVDVNIKDKLGNTPLLEAIKNGNDRVAALLVKEGATLSIENAGTFLCTVVAKGDSDFLKRLLNNGI DPNSKDYDQRTPLHVASSEGLYLLARQLVEAGANVLKKDRWGNTPLDEALVCGNKMLIKLLEDAKTSQMS TFLNSSKEIKDKVYKKKCTVYSSHPNDSKEKRRRGIVLWVPKSIEELVRSAAEQLNFPEASCVLSEDEGKIIDVE LISDGQKLYLTIET SEQ ID NO: 14> Brassica napus SKOR X1 mRNA ATGGGAGGTAGCAGCGGCGGCGGAGTTTCGTACCGGAGCGAAGTCGACTCGGACGTGGAGTTGGAG GATTACGAGGTGGATGATGATTTCGGAGAAGGCATCGTAGAATCGCGAGGAAACAGATTCAATCCCCT CACCAATTTCTTAGGATTAGATTTCACCGGAGGTAACGGCGGAAAGTTCACCGTCATTAACGGAATCAG AGATATCTCCAGAGGCTCCGTTGTTCATCCTGATAGCGGATGCTACAAGGCGTGGACCATGTTCATAGT GATATGGGCACTGTACTCTTCCTTCTTCACTCCATTGGAGTTCGGATTCTTCAGGGGATTACCAGGGAAT CTGTTCATCCTCGACATCCTTGGCCAAATCGCTTTCTTAGTCGATATTGTGTTAACATTCTTCGTGGCGTA TAGAGACAGCAGAACTTACAGAATGGTCTATAGACGCAGCTCCATCGCTTTACGCTACTTAAAATCAAC TTTTATTATTGATTTTCTATCATGTATGCCATGGGATATCATCTACAAGGTAGCAGGTCGAAAAGAAGAA GTGAGATACCTATTGTTGATAAGGCTATATCGAGTTCGAAGAGTGATCCTGTTTTTCCACAAAATGGAG AAAGACATAAGAATCAATTATCTTTTCACAAGAATCGTCAAGCTTATATTCGTCGAGCTCTATTGCACTC ACACCGCTGCTTGCATCTTCTATTACTTGGCCACCACGCTTCCTGCTTCTCAAGAAGGGTACACTTGGAT TGGAAGCTTGAAACTGGGGGATTACAGTTACGCTAAGTTTAGAGAGATCGATCTCTGGACCCGTTACA CCACTTCTATGTACTTCGCTGTTGTCACTATGGCAACTGTTGGTTATGGAGATATACATGCGGTTAACAT GCGGGAAATGATATTCGCGATGGCCTACATATCATTCGACATGATTCTAGGTGCTTACTTGATCGGTAA CATGACAGCTTTGATAGTAAAAGGCTCAAAAACAGAGAGATTCAGGGACAAGATGGCGGATATTATGA GGTATATGAACCGAAACAAACTCGGTAGAAACATCCGTGGTCAGATCACTGGTCATTTGCGGTTGCAG TACGAAAGTAGTTACACTGAAGCAGCTGTTCTTCAAGACATACCTGTCTCTATCCGCGCTAAGATTGCTC AAACGTTATATTTGTCGTATATTGAGAAAGTCCCTCTCTTCCGTGGATGCTCATCTGAATTCATTAACCA GATTGTTATAAGACTTCATGAAGAGTTTTTTCTCCCTGGAGAAGTAATAATGGAGCAAGGAAGTGTTGT TGATCAACTCTACTTCGTCTGTCATGGTGTATTGGAGGAGATAGGTACAGCTAAAGATGGATCTGAAGA GATAGTATCACTACTTCAACCAGATAACTCCTTTGGAGAGATTTCAATCCTCTGCAACATTCCTCAGCCTT ACACAGTTCGAGTTTCCGAGCTGTGTAGGGTTCTAAGGCTAGACAAACAATCTTTTATGAACATACTCG AGATATATTTCCACGATGGACGGAGGATACTCAACAATCTGCTTGAAGGGAAAGAATCTAACGGCAGG ATTAAGCAGCTGGAATCTGATATTACCTTTCATATCAGTAAACAAGAGGCAGAGCTAGCTTTGAAGTTG AATAGTGCTGCTTTCTATGGCGATCTTTATCAGCTTAAGAGCTTGATTCGAGCTGGAGCTGACCCAAAT AAAACAGATTATGATGGAAGATCGCCTTTGCATCTTGCAGCGTCTAGAGGATATGAAGACATCACACTG TATCTTATTCAAGAATCGGTAGACGTAAATATCAAAGATAAACTGGGGAACACGCCGTTACTAGAAGCA ATCAAGAACGGGAACGATCGTGTTGCGGCGTTGCTTGTGAAAGAAGGTGCAACGTTGAGCATAGAGA ACGCAGGGACTTTTCTTTGCACTGTGGTTGCCAAAGGAGACAGCGATTTCTTAAAACGTCTTCTCAACA ATGGCATTGATCCAAACTCTAAAGATTATGATCAGAGGACACCTCTTCACGTTGCTTCCTCTGAAGGGTT GTATCTCTTGGCAAGACAGTTGGTAGAAGCAGGTGCTAATGTTCTTAAAAAGGACAGGTGGGGAAATA CTCCTCTAGATGAAGCCCTAGTTTGTGGAAACAAGATGTTGATAAAACTACTTGAAGACGCTAAGACTT CTCAGATGTCTACGTTTCTGAATAGCTCTAAAGAGATCAAAGATAAAGTCTATAAGAAGAAATGCACAG TGTATTCTTCACATCCGAATGATTCCAAAGAGAAAAGAAGACGAGGGATTGTATTGTGGGTGCCTAAA 14051746-1 AGCATCGAGGAGCTTGTAAGAAGTGCAGCAGAACAGCTGAATTTTCCGGAAGCTTCTTGTGTTTTGTCT GAAGATGAAGGTAAAATTATTGATGTAGAGTTGATAAGTGATGGACAAAAACTGTATCTGACTATTGA AACATAA SEQ ID NO: 15>Raphanus sativus (Radish) SKOR XP_018491793.1 MGGSSGNGVSYRGEGESDVELEDYEVDDDDFRDGIVETRGNRFNPLTNFLGLDLAGGNGGKFTVINGIRDI SRGSVIHPDNRCYKAWTTFILIWALYSSFFTPLEFGFFRGLPENLFILDIAGQIAFLVDIVLTFFVAYRDSRTYRM VYRRSSIALRYLKSSFVIDLLACMPWDIIYKAAGEKEEVRYLLLIRLYRVRRVILFFHKMEKDIRINYLFTRIVKLIF VELYCTHTAACIFYYLATTLPASQEGYTWIGSLKLGDYSYAKFREIDLWTRYTTSMYFAIVTMATVGYGDIHA VNMREMIFAMIYISFDMILGAYLIGNMTALIVKGSKTERFRDKMADIMRYMNRNKLSRNIRGQITGHLRLQ YQSSYTEAAVLQDIPVSIRAKIAQTLYLPYIEKVPLFRGCSSEFINQIVIRLHEEFFLPGEVIMEQGSVVDQLYFV CHGVLEEIGTAKDGSEEIVSLLQPDNSFGEISILCNIPQPYTVRVSELCRILRLDKQSFMNILEIYFHDGRRILNN LLEGKESNVRIKELESDITFHISKQEGELALKLNSAAFYGDLYQLKSLIRAGADPNKTDYDGRSPLHLAASRGYE DITLYLIQESVDVNIKDKLGNTPLLEAIKNGNDRVAALLVKEGATLSIENAGTFLCTVVAKGDSDFLKRLLNNGI DPNSKDYDHRTPLHVAASEGLYLLAMQLVEAGANVLKKDRWGNTPLDEALGCGNKMLIKLLEDAKSSQISS FPSSSKELKDKVYKKKCTVYSSHPNDAKETRRRGIVLWVPRNIEELVRTAAEQLNVPEASCVLSEDEGKIIDVD LISDGQKLYLTVET* SEQ ID NO: 16>Raphanus sativus (Radish) SKOR mRNA ATGGGAGGCAGTAGCGGCAACGGAGTATCGTACCGGGGCGAGGGAGAATCTGACGTGGAGTTGGAG GATTACGAGGTGGATGATGATGACTTCAGAGATGGGATTGTAGAAACGCGAGGAAACAGATTCAACC CCCTCACGAACTTCCTAGGGTTAGATTTGGCCGGAGGTAACGGAGGAAAGTTCACCGTCATTAACGGA ATCAGAGATATCTCCAGAGGCTCCGTTATTCATCCCGATAACCGTTGCTACAAGGCGTGGACCACGTTC ATACTGATATGGGCACTTTACTCTTCCTTCTTTACTCCACTAGAATTTGGATTCTTCAGGGGACTACCAG AGAATCTATTCATCCTAGACATTGCAGGCCAAATCGCTTTCTTAGTCGATATCGTGCTAACGTTCTTCGT GGCTTATAGAGATAGCAGAACTTACAGAATGGTCTATAGACGCAGCTCCATCGCTCTACGGTACTTAAA ATCATCTTTTGTTATTGATTTACTTGCTTGCATGCCATGGGATATCATTTACAAGGCTGCAGGTGAAAAA GAAGAAGTGAGATACCTATTGTTGATAAGACTATATCGAGTTCGTAGAGTAATCCTGTTCTTCCACAAA ATGGAGAAAGACATAAGAATCAATTACCTTTTCACAAGAATCGTCAAGCTTATATTTGTTGAGCTCTATT GCACTCACACCGCGGCTTGTATCTTCTATTACCTGGCCACCACGCTACCTGCTTCTCAAGAAGGGTATAC TTGGATTGGAAGCTTGAAACTGGGAGATTACAGTTACGCTAAGTTTAGAGAGATCGATCTCTGGACTC GGTACACAACTTCTATGTACTTTGCAATTGTCACTATGGCAACTGTTGGTTATGGAGATATACATGCGGT TAATATGCGGGAAATGATATTTGCGATGATCTACATATCATTCGACATGATTCTAGGTGCTTACTTGATC GGTAACATGACAGCTTTGATAGTAAAAGGTTCAAAAACAGAGAGATTCAGGGACAAGATGGCGGATA TTATGAGGTATATGAACCGAAACAAACTCAGTAGAAACATCCGTGGTCAGATCACTGGACATTTACGGT TGCAGTACCAAAGTAGTTACACCGAGGCAGCTGTTCTTCAAGACATACCTGTCTCTATCCGCGCCAAGA TTGCACAAACTTTATACTTGCCATATATTGAGAAGGTTCCTCTCTTCCGTGGCTGCTCATCTGAGTTCATT AACCAGATTGTTATAAGACTTCATGAAGAGTTCTTTCTCCCTGGAGAAGTTATCATGGAGCAAGGAAGC GTTGTGGATCAGCTCTACTTTGTTTGTCATGGTGTTTTGGAGGAGATAGGTACAGCTAAGGATGGATCA GAAGAGATAGTGTCACTTCTTCAACCAGATAACTCTTTTGGAGAGATATCAATCCTCTGCAACATTCCTC AGCCTTACACAGTTCGAGTTTCTGAGCTGTGTCGGATTCTAAGACTAGATAAACAATCTTTCATGAACAT CCTCGAGATATATTTCCATGACGGAAGGAGGATCCTCAACAATCTGCTTGAAGGGAAAGAATCTAATGT CCGGATTAAGGAGCTGGAATCTGATATTACATTTCATATCAGTAAACAAGAGGGAGAGCTAGCTTTGA AGTTGAACAGTGCTGCTTTCTACGGTGATCTTTACCAGCTTAAGAGCTTGATTCGAGCTGGAGCTGACC CGAATAAGACAGATTATGACGGAAGATCACCTTTGCATCTTGCAGCCTCTAGAGGATATGAAGACATA ACATTGTACCTAATCCAAGAATCAGTAGATGTAAATATCAAAGATAAACTAGGGAACACGCCGTTACTA 14051746-1 GAAGCAATCAAGAACGGGAATGATCGTGTCGCGGCTTTGCTTGTGAAAGAAGGTGCAACGTTGAGCAT AGAGAACGCAGGGACTTTCCTTTGCACGGTGGTTGCTAAAGGAGACAGCGATTTCTTGAAACGTCTTCT CAACAACGGCATTGATCCTAACTCTAAAGACTATGATCACAGGACACCTCTCCACGTTGCTGCTTCTGAA GGATTGTATCTATTAGCAATGCAACTAGTAGAAGCAGGTGCTAATGTTCTTAAAAAAGACAGGTGGGG GAATACTCCTTTAGACGAAGCCCTAGGTTGTGGTAATAAGATGTTGATAAAACTACTTGAAGACGCTAA GAGTTCACAGATCTCTTCGTTTCCAAGTAGCTCCAAAGAGCTCAAAGATAAAGTATACAAGAAGAAATG TACAGTGTATTCTTCACATCCGAATGACGCAAAAGAAACAAGAAGACGTGGGATTGTGTTGTGGGTGC CTAGAAACATCGAGGAGCTTGTGAGAACTGCAGCAGAACAGTTGAATGTTCCTGAAGCTTCTTGTGTGT TGTCTGAAGATGAAGGTAAAATCATTGATGTAGATTTGATTAGTGATGGACAAAAGCTGTATCTGACCG TTGAAACATAA SEQ ID NO: 17>Glycine max SKOR XP_003544361.1 MTGKKNVKAATTTTPEEEDQRKQTTTSSSPSSSSRSSSSSSSSDEREYEVQDLRDRLKSSRGSRFDLIENQLGL NSTWSKFSRQALLHGIRGFSVDFVIHPDNRWYRAWTKFILLWAVYSSFFTPMEFGFFRGLPENLFILDIIGQI AFLVDIVLQFFVAYRDSQTYRTVYKRTPIALRYLKSNFIFDLLGCMPWDIIYKACGRKEEVRYLLWIRLYRVRKV TDFFHKLEKDIRVNYIITRIVKLIVVELYCTHTAACIFYYLATTLPESQEGYTWIGSLKLGDFSYSHFREIDLWKRY TTSLYFAIVTMATVGYGDIHAVNMREMVFIMVYVSFDMILGAYLIGNMTALIVKGSKTEKFRDKMTDLMKY MNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQTLYLPYIEKVSLFKGCSSEFIRQIVIRLHEEFF LPGEVIMEQGNVVDQLYFVCHGVLEEVGTAEDGTEETVSLLQPNSSFGEISILCNIPQPYTVRVCELSRLLRLD KQSFTNILDIYFYDGRKVLNNLLEGKESFRDKQLESDITFHIGKQEAELALKVNNAAFNGDLYQLKGLIRAGAD PNKTDYDGRSPLHLAASRGYEDITLFLIQERVDVNIKDNFGNTPLLEAVKNGHDRVASLLVREGASMKIENA GSFLCTAVARGDSDYLKRLLSNGMDPNLKDYDYRSPLHIAAAEGLYFMAKLLLEGGASVFTKDRWGNTPLD EARMCGNKNLIKLLEDAKSAQLSEFPSQEYTDKMHPKKCTVFPYHPWDPKDNRRHGIVLWIPHSIQELIKSA AEQIEFSGDACILSEDAGKVTDVDMIKDGQKLYLVHETH SEQ ID NO: 18>Glycine max SKOR XP_003544361.1 mRNA ATGACGGGGAAGAAGAATGTGAAGGCGGCGACAACCACGACACCGGAAGAGGAAGACCAGAGGAA GCAAACGACGACGTCGTCTTCCCCCTCGTCGTCTTCGCGCTCCTCCTCCTCGTCGTCGTCTTCGGATGAG AGAGAGTACGAGGTGCAGGACCTGCGTGACCGGTTGAAATCGTCGCGAGGGAGCAGGTTCGATCTCA TAGAGAACCAGTTGGGACTCAACTCGACTTGGAGCAAGTTCAGTCGCCAAGCGCTTCTCCATGGAATCC GAGGCTTCTCCGTGGACTTCGTTATTCATCCTGATAACAGGTGGTATCGGGCATGGACAAAATTCATAT TGCTATGGGCAGTGTATTCATCCTTCTTCACCCCAATGGAGTTTGGGTTTTTCCGTGGCCTGCCTGAGAA TCTCTTTATTCTGGACATCATTGGACAAATAGCTTTTCTTGTAGATATTGTCTTGCAATTTTTTGTTGCTTA TAGAGATAGTCAGACCTATCGTACGGTCTACAAGAGAACCCCTATTGCTCTGCGGTATCTGAAATCTAA CTTCATATTTGATCTTCTTGGATGTATGCCCTGGGACATCATCTACAAGGCTTGTGGAAGAAAAGAGGA AGTGAGATACCTTTTGTGGATCAGACTATATAGGGTTCGGAAAGTCACAGATTTTTTCCACAAGTTGGA GAAGGACATACGTGTCAATTACATTATTACCCGGATTGTGAAACTGATAGTAGTTGAACTCTATTGCAC CCATACAGCAGCCTGCATTTTCTACTATTTGGCTACCACACTACCTGAATCCCAAGAAGGGTACACATGG ATAGGAAGTTTAAAACTAGGTGACTTTAGTTATTCACATTTCAGAGAAATTGATCTTTGGAAGCGCTAT ACAACATCTCTGTACTTCGCTATTGTTACAATGGCTACAGTTGGCTATGGAGATATACATGCAGTAAATA TGAGGGAGATGGTATTCATAATGGTGTATGTTTCATTTGATATGATTCTTGGTGCCTATTTGATTGGTAA CATGACAGCTTTGATAGTCAAGGGATCAAAGACTGAAAAGTTTAGGGACAAGATGACAGACCTTATGA AATATATGAACAGAAATAGGCTTGGAAGGGATATCCGTGAACAAATTAAGGGCCATGTGCGGTTACAG TATGAGAGTAGCTACACTGAGGCTTCTGTCATTCAGGATATCCCTATATCTATTCGAGCTAAGATATCCC AAACATTATATTTGCCGTACATTGAAAAGGTTTCTCTTTTTAAGGGATGCTCTTCTGAATTCATCCGTCA GATTGTTATTAGGCTCCATGAGGAGTTCTTTCTTCCAGGGGAAGTTATAATGGAACAAGGAAATGTTGT 14051746-1 GGATCAACTATATTTTGTCTGCCATGGAGTACTGGAGGAAGTAGGCACTGCTGAAGATGGGACTGAAG AAACTGTTTCACTTCTGCAGCCTAACAGTTCATTCGGAGAAATATCTATTCTTTGCAACATTCCTCAACCA TATACTGTCCGTGTTTGTGAACTGAGTAGACTCCTGCGACTTGATAAACAATCATTTACAAATATCCTAG ACATATACTTTTATGATGGAAGGAAAGTATTAAACAACCTTCTAGAGGGAAAAGAATCTTTTCGAGATA AGCAGTTGGAGTCAGACATCACATTTCATATTGGAAAGCAAGAAGCTGAGCTTGCTTTGAAGGTCAAT AATGCAGCTTTCAATGGGGATCTGTATCAGCTAAAAGGTTTAATTCGCGCTGGAGCTGATCCCAACAAG ACAGATTATGATGGAAGGTCACCTTTGCATCTTGCAGCATCTAGAGGATATGAAGATATCACACTTTTC CTTATTCAAGAACGTGTAGATGTCAATATTAAAGATAACTTCGGGAACACACCCTTACTTGAAGCAGTT AAGAATGGACATGATCGGGTTGCTTCTTTACTTGTTAGAGAAGGGGCCTCTATGAAGATTGAAAATGCT GGTAGTTTTTTGTGTACTGCAGTTGCAAGGGGAGATTCAGATTATCTTAAAAGACTTTTATCCAATGGC ATGGATCCTAACTTAAAAGATTATGATTACCGAAGTCCTCTTCACATTGCTGCAGCTGAAGGTTTATATT TCATGGCAAAGTTGCTATTAGAAGGAGGAGCTAGTGTTTTTACCAAAGACAGATGGGGAAATACGCCG CTTGATGAAGCTCGGATGTGTGGAAATAAGAACCTGATCAAGCTTCTGGAAGATGCAAAATCTGCTCA ACTGTCAGAATTCCCATCCCAAGAATATACAGACAAAATGCATCCAAAGAAGTGCACAGTGTTCCCTTA CCACCCGTGGGATCCGAAAGATAATAGAAGACATGGAATTGTATTATGGATTCCACACTCCATACAAGA GCTAATCAAATCAGCGGCAGAACAAATAGAATTTTCTGGCGATGCTTGTATTTTATCAGAAGATGCTGG TAAAGTTACTGATGTGGACATGATCAAGGATGGTCAGAAGCTGTATTTAGTCCATGAAACACATTAG SEQ ID NO: 19>Solanum lycopersicum SKOR XP_004240037.1 MSMKRELREERNGRDSPKEYKMDDLRDSMKSLRSTSRLAMMENELIADSTPWRFSSENVLNGLRGLSQGF VIYPDDRWYKLWDKFILIWAIYSTFFTPMEFGFFKGLPRKLFLLDICGQIAFLVDIVIQFFVAYRDSQTYKMVY RRTPIALRYLKSHFILDVLSCMPWDNIYKASGRKEGVRYLLWIRLSRVRRVTDFFQKMEKDIRINYLFTRIVKLI TVELYCTHTAACIFYFLATTLPEEKEGYTWIGSLTLGDYSYSHFREIDLWRRYITSLYFAIVTMATVGYGDIHAV NLREMIFVMVYVSFDMILGAYLIGNMTALIVKGSKTVRYRDKMTDLMNYMNRNRLGRDIRSQIKDHLRLQ YESAYTDGAVLQDLPISIRAKISQTLYLSCIENIPLFRECSAEFISQIVTRVHEEFFLPGEVIMEQGHVVDQLYFV CDGVLEEVGIGEDGSQETVALLEPNSSFGEISILCNIPQPYTVRVSELCRLIRIDKQSFSNILEIYFHDGRRILTNL LEGKDLRVKQLESDITFHIGKQEAELALKVNSAAYHGDLHQLKSLIRAGADPNKKDYDGRSPLHLSASRGYED ISIFLIKEGVDFNASDNFGNTPLFEAIKNGHDRVASLLVKEGAFLKIENAGSFLCTLVTKGDSDLLRRLLSNGID ANSKDYDHRTPLHVAASQGLLAMARLLLGAGASVFSKDRWGNTPFDEARLSGNNQLIKLLEEAKSAQTSEI HSVSHEISEKIHLRKCTVYPIHPWEPKDLRKHGVVLWVPTSMEELVTAASEQLNFSSGSCILSEDAGKILDIDM ISDGQKLYLISETT SEQ ID NO: 20>Solanum lycopersicum SKOR mRNA ATGTCGATGAAGAGAGAATTACGAGAAGAGAGAAATGGAAGAGATTCACCAAAAGAGTATAAAATGG ATGATTTGAGAGATAGTATGAAATCGTTGCGAAGTACCAGTCGATTGGCGATGATGGAAAACGAGCTA ATTGCCGATTCAACTCCTTGGAGATTTAGCAGTGAAAACGTCCTCAATGGCCTCAGAGGCCTTTCTCAA GGTTTCGTCATTTATCCCGATGACAGGTGGTACAAGCTATGGGATAAGTTTATCCTGATTTGGGCTATA TATTCAACTTTTTTTACACCAATGGAGTTTGGATTCTTCAAAGGATTGCCCAGGAAACTATTTCTTTTAGA CATTTGTGGTCAAATAGCTTTTCTTGTCGACATAGTCATACAATTTTTTGTAGCCTACAGAGACAGTCAG ACATACAAGATGGTGTATAGGCGAACCCCTATTGCTCTCCGGTACTTGAAATCTCATTTTATCTTGGATG TGCTCAGTTGCATGCCGTGGGATAACATTTATAAGGCTTCTGGCAGAAAAGAAGGAGTGAGATACCTT TTATGGATTAGATTAAGCAGGGTGCGGAGGGTTACTGACTTTTTCCAGAAGATGGAGAAAGATATTCG GATCAATTATCTCTTCACTAGGATTGTAAAGCTTATCACTGTTGAACTTTATTGCACGCATACAGCAGCT TGCATCTTTTACTTTCTGGCAACTACTCTGCCTGAAGAGAAAGAAGGCTACACATGGATTGGTAGTTTG ACCCTGGGAGATTACAGTTATTCACACTTTAGAGAGATTGATCTCTGGAGGCGGTACATCACTTCCCTG TACTTTGCAATTGTCACTATGGCAACTGTGGGTTATGGTGACATACATGCAGTCAATCTGAGGGAAATG 14051746-1 ATATTTGTAATGGTTTATGTCTCTTTTGATATGATTCTTGGTGCTTACTTGATCGGTAACATGACAGCATT GATTGTCAAGGGATCAAAAACTGTGCGATACAGGGACAAAATGACAGATCTTATGAACTATATGAACA GAAATAGACTCGGAAGGGATATTCGTAGTCAAATTAAAGATCACTTGCGATTACAATATGAAAGCGCTT ACACTGATGGAGCCGTTCTCCAGGACCTTCCCATCTCAATTCGTGCAAAGATATCCCAGACTTTATATCT GTCTTGCATTGAAAATATTCCTCTTTTCAGGGAGTGCTCCGCAGAATTCATAAGTCAAATTGTAACTCGA GTGCATGAAGAATTTTTCCTCCCAGGAGAAGTGATCATGGAACAGGGGCATGTAGTGGACCAACTTTA TTTTGTCTGTGATGGTGTGCTGGAAGAAGTTGGTATAGGAGAAGATGGGTCACAAGAGACAGTAGCAC TTCTTGAACCTAATAGCTCGTTTGGAGAAATATCCATTCTTTGCAACATTCCACAGCCATATACTGTCCGT GTTAGTGAACTATGCAGACTCATACGGATTGATAAGCAATCATTTTCAAATATTTTGGAGATCTATTTTC ATGATGGAAGAAGAATCTTGACGAACTTACTAGAGGGAAAGGATCTTCGTGTGAAGCAACTGGAGTCA GATATAACATTCCATATTGGGAAACAAGAGGCTGAGCTTGCTTTGAAAGTGAATAGTGCAGCTTATCAT GGTGATTTGCACCAGCTGAAGAGTCTGATTCGAGCTGGAGCTGATCCCAACAAGAAAGATTATGATGG AAGATCACCTCTGCATCTTTCAGCATCCAGAGGATATGAAGACATCTCTATTTTCCTTATCAAAGAAGGT GTCGATTTCAATGCTTCAGACAACTTTGGAAACACACCGCTCTTTGAAGCTATCAAGAATGGACACGAT CGTGTTGCTTCATTACTTGTTAAGGAAGGTGCCTTCTTGAAGATTGAAAATGCTGGTAGCTTCTTGTGCA CATTGGTTACAAAAGGGGATTCAGATCTACTACGAAGGCTGTTGTCCAACGGTATTGATGCAAACTCCA AAGATTATGATCACCGAACACCGCTCCATGTAGCGGCTTCTCAAGGATTACTCGCAATGGCGAGATTGC TTCTGGGAGCTGGTGCTTCAGTTTTTTCAAAGGACAGATGGGGAAATACTCCATTTGATGAAGCTAGAC TAAGTGGAAACAATCAGTTGATCAAGCTTCTGGAAGAAGCAAAATCTGCTCAAACATCGGAAATCCAC AGTGTTTCACACGAGATTTCAGAAAAAATTCACCTGCGGAAGTGTACTGTATACCCTATCCACCCATGG GAGCCTAAGGACCTCAGGAAACATGGTGTTGTTTTATGGGTACCTACGAGTATGGAAGAGCTCGTTAC TGCAGCTTCGGAACAACTCAACTTCTCATCAGGCTCTTGTATTTTATCAGAAGATGCAGGTAAAATTCTT GATATAGATATGATATCTGATGGTCAGAAGTTGTACTTGATCAGTGAAACAACTTGA SEQ ID NO: 21>Solanum tuberosum SKOR XP_006360380.1 MSMKRELGEERNGRDSPKEYKMNDLRDSMKSLRSTSRLAMMENELIADSTPSRFSRENVINGLRGLSQDF VIYPDDRWYKLWDKFILIWAIYSTFFTPMEFAFFKGLPRKLFLLDICGQIAFLVDIVIQFFVAYRDSQTYKMVY RRTPIALRYLKSHFILDVLSCMPWDNIFKASGRIEGVRYLLWIRLSRVRRVTDFFQKMEKDIRINYLFTRIIKLIT VELYCTHTAACIFYFLATTLPAEKEGYTWIGSLTLGDYSYSNFREIDLWRRYITSLYFAIVTMATVGYGDIHAVN LREMIFVMVYVSFDMILGAYLIGNMTALIVKGSKTVRYRDKMTDLMNYMNRNRLGRDIRSQIKDHLRLQYE SAYTDGAVLHDLPISIRAKISQTLYQSCIENIPLFRECSAEFISQIVTRVHEEFFLPGEVIMEQGHVVDQLYFVCD GVLVEVGIGEDGSQETVAHLEPNSSFGEISILCNIPQPYTVRVCELCRLIRIDKQSFSNILEIYFHDGRRILANLLE GKDLRVKQLESDITFHIGKQEADLALKVNSAAYHGDLHQLKSLIRAGADPNKKDYDGRSPLHLSASRGYEDIS FFLVKEGIDLNASDNFGNTPLFEAIKNGHDRVASLLVKEGAFLKIENAGSFLCTLVTKGDSDLLRRLLSNGIDA NSKDYDHRTPLHVAASQGLLAMARLLLGAGASVFSMDRWGNTPFDEARLSGNNQLIKLLEDAKSAQTSEF PSVSHEISEKKHPRKCTVFPVHPWEPKDLRKHGVVLWVPTSMEELVTAASEQLNFPSGSCILSEDAGKILDID MISDGQKLYLISETT SEQ ID NO: 22 >Solanum tuberosum SKOR mRNA ATGTCGATGAAGAGAGAATTAGGAGAAGAGAGGAATGGAAGAGATTCACCAAAAGAGTATAAGATG AATGATTTGAGAGATAGTATGAAATCGTTGAGAAGTACCAGTAGATTAGCGATGATGGAGAACGAGCT AATAGCTGATTCAACTCCTTCGAGATTTAGCAGAGAAAACGTCATCAATGGCCTCAGAGGCCTTTCTCA AGATTTCGTCATTTATCCCGATGACAGGTGGTACAAGCTATGGGATAAGTTTATCCTGATTTGGGCAAT ATATTCAACTTTTTTTACACCAATGGAGTTTGCATTCTTTAAAGGATTGCCCAGGAAACTATTTCTTTTAG ACATTTGTGGTCAAATAGCTTTTCTTGTCGACATAGTCATACAATTTTTTGTAGCCTACAGAGATAGTCA GACATACAAGATGGTGTATAGGCGAACCCCTATTGCTCTTCGGTACTTGAAATCTCATTTTATCTTGGAT GTTCTCAGTTGCATGCCGTGGGATAACATTTTTAAGGCTTCTGGAAGAATTGAAGGAGTGAGATACCTT 14051746-1 TTATGGATTAGGTTAAGCAGGGTGCGCAGGGTTACTGACTTTTTCCAGAAGATGGAGAAAGATATTCG AATCAATTATCTCTTCACTAGGATTATAAAGCTTATCACTGTTGAACTTTATTGCACGCATACAGCAGCTT GCATCTTTTACTTTTTGGCAACTACTCTGCCTGCAGAGAAAGAAGGCTACACATGGATTGGTAGTTTGA CCCTGGGAGATTACAGTTATTCAAACTTTAGAGAGATTGATCTCTGGAGGCGGTACATCACTTCTCTGT ACTTTGCAATTGTCACTATGGCAACTGTGGGTTATGGTGACATACATGCAGTCAATCTGAGGGAAATGA TATTTGTGATGGTTTATGTTTCTTTTGATATGATTCTTGGTGCTTACTTGATCGGTAACATGACAGCACTG ATTGTCAAGGGATCAAAAACTGTGCGATACAGGGACAAAATGACAGATCTTATGAACTATATGAACAG AAATAGACTCGGAAGGGATATTCGTAGTCAAATTAAAGATCACTTGCGATTACAATATGAAAGCGCTTA CACTGATGGAGCCGTTCTCCATGACCTTCCCATCTCAATTCGTGCCAAGATATCCCAGACTTTATATCAG TCTTGCATTGAAAATATTCCTCTTTTTAGGGAGTGCTCCGCAGAATTCATAAGTCAAATTGTAACTCGAG TGCATGAAGAATTTTTCCTCCCAGGAGAAGTGATCATGGAACAGGGGCATGTAGTGGACCAACTTTATT TTGTCTGTGATGGTGTCCTGGTAGAAGTTGGTATAGGAGAAGATGGGTCACAAGAGACAGTAGCACAT CTTGAGCCTAATAGCTCGTTCGGAGAAATATCCATTCTTTGCAACATTCCACAACCATATACTGTCCGTG TTTGTGAACTATGCAGACTCATACGGATTGATAAGCAGTCATTTTCAAATATTTTGGAGATCTATTTTCA CGATGGAAGAAGAATCTTGGCGAACTTACTAGAGGGAAAGGATCTTCGTGTGAAGCAACTGGAGTCA GATATAACATTCCATATTGGGAAACAAGAGGCTGATCTTGCTTTGAAAGTTAATAGTGCAGCTTATCAT GGTGACTTACACCAGCTGAAGAGTCTTATTCGAGCTGGAGCTGATCCCAACAAGAAAGATTATGATGG AAGATCACCTCTGCATCTTTCAGCATCCAGAGGATATGAAGACATCTCTTTTTTCCTTGTCAAAGAAGGT ATCGATCTCAATGCTTCAGACAACTTTGGAAACACACCGCTCTTTGAAGCTATCAAGAATGGACACGAT CGTGTTGCTTCATTACTTGTTAAGGAAGGTGCCTTCTTGAAGATTGAAAATGCTGGTAGCTTCTTGTGTA CGTTGGTTACAAAAGGGGATTCAGATCTACTACGAAGGCTGTTGTCCAATGGTATTGATGCAAACTCCA AAGATTATGATCACCGAACACCGCTCCATGTAGCGGCTTCTCAAGGATTGCTTGCGATGGCGAGATTGC TTCTGGGAGCTGGTGCTTCAGTTTTTTCAATGGACAGATGGGGAAATACTCCATTTGATGAAGCTAGAC TAAGTGGAAACAATCAGTTGATCAAGCTTCTGGAAGACGCAAAATCAGCTCAAACATCAGAATTCCCCA GTGTTTCGCATGAGATTTCAGAAAAAAAGCACCCACGGAAGTGTACTGTATTCCCTGTCCACCCATGGG AGCCCAAGGACCTCAGGAAACATGGTGTTGTACTATGGGTACCTACGAGTATGGAAGAGCTCGTTACT GCAGCTTCAGAACAACTCAACTTCCCATCAGGCTCTTGTATTTTATCAGAAGATGCAGGTAAAATTCTTG ATATAGATATGATATCTGATGGTCAGAAGTTGTACTTGATCAGTGAAACAACTTGA SEQ ID NO: 23 PNNP MGRLRRRQEIIDHEEEESNDDVSSDDGDLSLAKTFDWLKSSKDDDIKTKGDNKYDYIIDPKNRW YKAWEMFILVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQTYRTVY KPTRIAFRYLKSHFLMDFIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRIN YLFTRILKLLFVEVYCTHTAACIFYYLATTLPPENEGYTWIGSLKLGDYSYENFREIDLWKRYTTA LYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNITALIVKGSNTERFRDKMNDLIS FMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCSTE FINQIVIRLHEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISII CNISQPFTVRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQ EAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVN LKDKFGHTPLFEAVKAGQEGVIGLLAKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMDP NSEDYDHRTPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDTK NAQSSIYPTSLRELQEERIERRKCTVFPFHPQEAKEERSRKHGVVVWIPSNLEKLIVTAAKELGL SDGASFVLLSEDQGRITDIDMISDGHKLYMISDTTDQTHPAFLYKVVMGRPRRSTRVDSRYPTS SEQ ID NO: 24 PNNP 14051746-1 atgggacgtctccggagacggcaagagataatagatcatgaagaagaggaatcaaacgacgacgtttcatcagatgatggagatc tcagtttagccaaaacgtttgattggcttaaatcatcaaaagatgatgatattaaaaccaaaggtgataataaatatgattacatcattgat cccaaaaacaggtggtacaaggcatgggaaatgtttatattggtgtgggcaatatactcctcattgttcactcccatggagtttggtttcttc cgcggtctgcctgagagactctttgtacttgacattgttggtcagatcgcgttcttggtcgatattgttcttcagttctttgttgcctatcgcgata ctcagacctaccggactgtctacaaaccaacacgtattgctttccggtacttgaagtcgcattttctcatggatttcatcggttgcttcccttg ggatcttatttataaggcatcagggaaacatgagttggtgaggtacttgttgtggataaggctatttcgggttcgcaaagtggttgagttttt ccaaaggcttgagaaagacacaagaatcaactatctattcactagaatcttaaagctcttgttcgttgaagtttattgtactcacactgctg cttgtatcttctattacttggccaccactcttcctccggaaaacgaaggttacacttggatcggtagcttgaagctaggagactatagctac gagaatttccgagaaatcgatctatggaaacgttatactactgctctatacttcgccattgtcactatggcaactgtcggttatggagacat tcacgcggtgaatctgagggaaatgatatttgtaatgatatatgtttcatttgatatggttctcggtgcttaccttattggtaacatcactgcctt gattgtgaaaggttcaaacacagagaggttcagagataaaatgaatgatctcataagtttcatgaaccgcaaaaaactcgggagag accttcgtagccagataactggtcatgttagattgcagtacgacagtcactacaccgacactgtcatgcttcaggacatcccagcatca atccgcgccaagattgcgcaattattgtatctgccttacatcaaaaaagttcctctcttcaaaggctgctccacagagtttattaatcaaat agttataaggctccatgaagagtattttcttccaggagaagtaataacagagcaaggaaacgtcgtggatcatttgtatttcgtctgtgaa ggcttactggaggctcttgttacaaaaacagatggatcagaagagagtgtgacgttacttgggcctcacacttcttttggagacatctcc atcatttgcaacatttctcaacctttcactgttagggtttgtgagctatgccatcttttacgactcgataaacagtctttctcaaacatcctcga gatttattttcacgacggacgcacaatcttgaacaatattatggaggagaaggaatcaaatgataggataaagaagctagaatctgac atagtgattcacattgggaaacaagaagcagaacttgcattgaaagtaaacagtgcagctttccaaggagatttttaccagcttaaga gcttaatccgatctggagccgatcctaacaaaaccgattacgatggaagatcaccgcttcatcttgcggcatgtagaggctatgaaga cattacattattccttattcaagaaggtgttgatgtcaatctaaaagataagttcggacacacaccattgtttgaggctgtgaaagcagga caagaaggagtgattggtttgcttgccaaagaaggagcctcctttaatttagaagattcaggaaacttcctttgcacgacagttgctaaa ggcgactctgattttctcaagagattgctttcaagcggtatggacccaaacagtgaagattatgatcacagaacgccgcttcatgtcgcg gcttctgaagggttattcttgatggctaaaatgttggttgaagctggagcaagcgttatttctaaagaccggtgggggaattctccgcttga tgaagctcgattgtgcggaaacaagaaactgattaagttactcgaagatacgaaaaatgctcagtcgtctatctacccgacaagcttg cgtgaattacaagaggagagaattgagagacggaaatgcacggtgtttccattccacccgcaagaggcgaaagaagagcgtagt agaaagcacggagttgtggtttggatcccaagcaatctcgagaaactcatagtaaccgctgcgaaagagctagggctatcggatgg agcctcatttgtactattatccgaagaccaaggtcgtatcacagacattgatatgattagtgatggacacaaattgtatatgatcagtgat actactgatcaaaca SEQ ID NO: 25 NP atgggacgtctccggagacggcaagagataatagatcatgaagaagaggaatcaaacgacgacgtttcatcaagaagaggaaa actcagtttagccaaaacgtttcggtggcttaaatcatcaaaaaaacggagaattaaaaccaaaggtaaaaataaatataaatacat cattaaacccaaaaacaggtggtacaaggcatgggaaatgtttatattggtgtgggcaatatactcctcattgttcactcccatggagttt ggtttcttccgcggtctgcctgagagactctttgtacttgacattgttggtcagatcgcgttcttggtcgatattgttcttcagttctttgttgcctat cgcgatactcagacctaccggactgtctacaaaccaacacgtattgctttccggtacttgaagtcgcattttctcatggatttcatcggttgc ttcccttgggatcttatttataaggcatcagggaaacatgagttggtgaggtacttgttgtggataaggctatttcgggttcgcaaagtggtt gagtttttccaaaggcttgagaaagacacaagaatcaactatctattcactagaatcttaaagctcttgttcgttgaagtttattgtactcac actgctgcttgtatcttctattacttggccaccactcttcctccggaaaacgaaggttacacttggatcggtagcttgaagctaggagacta 14051746-1 tagctacgagaatttccgagaaatcgatctatggaaacgttatactactgctctatacttcgccattgtcactatggcaactgtcggttatg gagacattcacgcggtgaatctgagggaaatgatatttgtaatgatatatgtttcatttgatatggttctcggtgcttaccttattggtaacatc actgccttgattgtgaaaggttcaaacacagagaggttcagagataaaatgaatgatctcataagtttcatgaaccgcaaaaaactcg ggagagaccttcgtagccagataactggtcatgttagattgcagtacgacagtcactacaccgacactgtcatgcttcaggacatccc agcatcaatccgcgccaagattgcgcaattattgtatctgccttacatcaaaaaagttcctctcttcaaaggctgctccacagagtttatta atcaaatagttataaggctccatgaagagtattttcttccaggagaagtaataacagagcaaggaaacgtcgtggatcatttgtatttcgt ctgtgaaggcttactggaggctcttgttacaaaaacagatggatcagaagagagtgtgacgttacttgggcctcacacttcttttggaga catctccatcatttgcaacatttctcaacctttcactgttagggtttgtgagctatgccatcttttacgactcgataaacagtctttctcaaacat cctcgagatttattttcacgacggacgcacaatcttgaacaatattatggaggagaaggaatcaaatgataggataaagaagctaga atctgacatagtgattcacattgggaaacaagaagcagaacttgcattgaaagtaaacagtgcagctttccaaggagatttttaccagc ttaagagcttaatccgatctggagccgatcctaacaaaaccgattacgatggaagatcaccgcttcatcttgcggcatgtagaggctat gaagacattacattattccttattcaagaaggtgttgatgtcaatctaaaagataagttcggacacacaccattgtttgaggctgtgaaag caggacaagaaggagtgattggtttgcttgccaaagaaggagcctcctttaatttagaagattcaggaaacttcctttgcacgacagttg ctaaaggcgactctgattttctcaagagattgctttcaagcggtatggacccaaacagtgaagattatgatcacagaacgccgcttcat gtcgcggcttctgaagggttattcttgatggctaaaatgttggttgaagctggagcaagcgttatttctaaagaccggtgggggaattctc cgcttgatgaagctcgattgtgcggaaacaagaaactgattaagttactcgaagatacgaaaaatgctcagtcgtctatctacccgac aagcttgcgtgaattacaagaggagagaattgagagacggaaatgcacggtgtttccattccacccgcaagaggcgaaagaaga gcgtagtagaaagcacggagttgtggtttggatcccaagcaatctcgagaaactcatagtaaccgctgcgaaagagctagggctatc ggatggagcctcatttgtactattatccgaagaccaaggtcgtatcacagacattgatatgattagtgatggacacaaattgtatatgatc agtgatactactgatcaaaca SEQ ID NO: 26 NP MGRLRRRQEIIDHEEEESNDDVSSRRGKLSLAKTFRWLKSSKKRRIKTKGKNKYKYIIKPKNRW YKAWEMFILVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQTYRTVY KPTRIAFRYLKSHFLMDFIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRIN YLFTRILKLLFVEVYCTHTAACIFYYLATTLPPENEGYTWIGSLKLGDYSYENFREIDLWKRYTTA LYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNITALIVKGSNTERFRDKMNDLIS FMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCSTE FINQIVIRLHEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISII CNISQPFTVRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQ EAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVN LKDKFGHTPLFEAVKAGQEGVIGLLAKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMDP NSEDYDHRTPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDTK NAQSSIYPTSLRELQEERIERRKCTVFPFHPQEAKEERSRKHGVVVWIPSNLEKLIVTAAKELGL SDGASFVLLSEDQGRITDIDMISDGHKLYMISDTTDQTHPAFLYKVVMGRPRRSTRVDSRYPTS SEQ ID NO: 27 kN-gS1-L4 atgtcgatctcttggactcgaaatttcttcgaaagattctgcgtcgaggaatacaatatagacaccataaaacagagtagtttcctctctg ccgatcttctaccatctcttggagccaggatcaaccaatctactaagctccgcaaacacataatctctcccaaaaacaggtggtacaa 14051746-1 ggcatgggaaatgtttatattggtgtgggcaatatactcctcattgttcactcccatggagtttggtttcttccgcggtctgcctgagagactc tttgtacttgacattgttggtcagatcgcgttcttggtcgatattgttcttcagttctttgttgcctatcgcgatactcagacctaccggactgtcta caaaccaacacgtattgctttccggtacttgaagtcgcattttctcatggatttcatcggttgcttcccttgggatcttatttataaggcatcag ggaaacatgagttggtgaggtacttgttgtggataaggctatttcgggttcgcaaagtggttgagtttttccaaaggcttgagaaagacac aagaatcaactatctattcactagaatcttaaagctcttgttcgttgaagtttattgtactcacactgctgcttgtatcttctattacttggccacc actcttcctccggaaaacgaaggttacacttggatcggtagcttgaagctaggagactatagctacgagaatttccgagaaatcgatct atggaaacgttatactactgctctatacttcgccattgtcactatggcaactgtcggttatggagacattcacgcggtgaatctgagggaa atgatatttgtaatgatatatgtttcatttgatatggttctcggtgcttaccttattggtaacatcactgccttgattgtgaaaggttcaaacaca gagaggttcagagataaaatgaatgatctcataagtttcatgaaccgcaaaaaactcgggagagaccttcgtagccagataactggt catgttagattgcagtacgacagtcactacaccgacactgtcatgcttcaggacatcccagcatcaatccgcgccaagattgcgcaatt attgtatctgccttacatcaaaaaagttcctctcttcaaaggctgctccacagagtttattaatcaaatagttataaggctccatgaagagt attttcttccaggagaagtaataacagagcaaggaaacgtcgtggatcatttgtatttcgtctgtgaaggcttactggaggctcttgttaca aaaacagatggatcagaagagagtgtgacgttacttgggcctcacacttcttttggagacatctccatcatttgcaacatttctcaaccttt cactgttagggtttgtgagctatgccatcttttacgactcgataaacagtctttctcaaacatcctcgagatttattttcacgacggacgcac aatcttgaacaatattatggaggagaaggaatcaaatgataggataaagaagctagaatctgacatagtgattcacattgggaaaca agaagcagaacttgcattgaaagtaaacagtgcagctttccaaggagatttttaccagcttaagagcttaatccgatctggagccgatc ctaacaaaaccgattacgatggaagatcaccgcttcatcttgcggcatgtagaggctatgaagacattacattattccttattcaagaag gtgttgatgtcaatctaaaagataagttcggacacacaccattgtttgaggctgtgaaagcaggacaagaaggagtgattggtttgcttg ccaaagaaggagcctcctttaatttagaagattcaggaaacttcctttgcacgacagttgctaaaggcgactctgattttctcaagagatt gctttcaagcggtatggacccaaacagtgaagattatgatcacagaacgccgcttcatgtcgcggcttctgaagggttattcttgatggc taaaatgttggttgaagctggagcaagcgttatttctaaagaccggtgggggaattctccgcttgatgaagctcgattgtgcggaaaca agaaactgattaagttactcgaagatacgaaaaatgctcagtcgtctatctacccgacaagcttgcgtgaattacaagaggagagaat tgagagacggaaatgcacggtgtttccattccacccgcaagaggcgaaagaagagcgtagtagaaagcacggagttgtggtttgg atcccaagcaatctcgagaaactcatagtaaccgctgcgaaagagctagggctatcggatggagcctcatttgtactattatccgaag accaaggtcgtatcacagacattgatatgattagtgatggacacaaattgtatatgatcagtgatactactgatcaaaca SEQ ID NO: 28 kN-gS1-L4 MSISWTRNFFERFCVEEYNIDTIKQSSFLSADLLPSLGARINQSTKLRKHIISPKNRWYKAWEMFI LVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQTYRTVYKPTRIAFR YLKSHFLMDFIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRINYLFTRILKL LFVEVYCTHTAACIFYYLATTLPPENEGYTWIGSLKLGDYSYENFREIDLWKRYTTALYFAIVTM ATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNITALIVKGSNTERFRDKMNDLISFMNRKKL GRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCSTEFINQIVIRL HEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISIICNISQPFT VRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQEAELALKV NSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVNLKDKFGHT PLFEAVKAGQEGVIGLLAKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMDPNSEDYDHR TPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDTKNAQSSIYPT 14051746-1 SLRELQEERIERRKCTVFPFHPQEAKEERSRKHGVVVWIPSNLEKLIVTAAKELGLSDGASFVLL SEDQGRITDIDMISDGHKLYMISDTTDQTHPAFLYKVVMGRPRRSTRVDSRYPTS SEQ ID NO: 29 PN atgggacgtctccggagacggcaagagataatagatcatgaagaagaggaatcaaacgacgacgtttcatcagatgatggagatc tcagtttagccgagacgtttgattggcttgattcatcagaggacgatgatattgaaaccgatggtgataatgattatgattacatcattgatc ccaaaaacaggtggtacaaggcatgggaaatgtttatattggtgtgggcaatatactcctcattgttcactcccatggagtttggtttcttcc gcggtctgcctgagagactctttgtacttgacattgttggtcagatcgcgttcttggtcgatattgttcttcagttctttgttgcctatcgcgatact cagacctaccggactgtctacaaaccaacacgtattgctttccggtacttgaagtcgcattttctcatggatttcatcggttgcttcccttggg atcttatttataaggcatcagggaaacatgagttggtgaggtacttgttgtggataaggctatttcgggttcgcaaagtggttgagtttttcca aaggcttgagaaagacacaagaatcaactatctattcactagaatcttaaagctcttgttcgttgaagtttattgtactcacactgctgcttg tatcttctattacttggccaccactcttcctccggaaaacgaaggttacacttggatcggtagcttgaagctaggagactatagctacgag aatttccgagaaatcgatctatggaaacgttatactactgctctatacttcgccattgtcactatggcaactgtcggttatggagacattcac gcggtgaatctgagggaaatgatatttgtaatgatatatgtttcatttgatatggttctcggtgcttaccttattggtaacatcactgccttgatt gtgaaaggttcaaacacagagaggttcagagataaaatgaatgatctcataagtttcatgaaccgcaaaaaactcgggagagacct tcgtagccagataactggtcatgttagattgcagtacgacagtcactacaccgacactgtcatgcttcaggacatcccagcatcaatcc gcgccaagattgcgcaattattgtatctgccttacatcaaaaaagttcctctcttcaaaggctgctccacagagtttattaatcaaatagtta taaggctccatgaagagtattttcttccaggagaagtaataacagagcaaggaaacgtcgtggatcatttgtatttcgtctgtgaaggctt actggaggctcttgttacaaaaacagatggatcagaagagagtgtgacgttacttgggcctcacacttcttttggagacatctccatcatt tgcaacatttctcaacctttcactgttagggtttgtgagctatgccatcttttacgactcgataaacagtctttctcaaacatcctcgagatttat tttcacgacggacgcacaatcttgaacaatattatggaggagaaggaatcaaatgataggataaagaagctagaatctgacatagtg attcacattgggaaacaagaagcagaacttgcattgaaagtaaacagtgcagctttccaaggagatttttaccagcttaagagcttaat ccgatctggagccgatcctaacaaaaccgattacgatggaagatcaccgcttcatcttgcggcatgtagaggctatgaagacattaca ttattccttattcaagaaggtgttgatgtcaatctaaaagataagttcggacacacaccattgtttgaggctgtgaaagcaggacaagaa ggagtgattggtttgcttgccaaagaaggagcctcctttaatttagaagattcaggaaacttcctttgcacgacagttgctaaaggcgact ctgattttctcaagagattgctttcaagcggtatggacccaaacagtgaagattatgatcacagaacgccgcttcatgtcgcggcttctga agggttattcttgatggctaaaatgttggttgaagctggagcaagcgttatttctaaagaccggtgggggaattctccgcttgatgaagct cgattgtgcggaaacaagaaactgattaagttactcgaagatacgaaaaatgctcagtcgtctatctacccgacaagcttgcgtgaatt acaagaggagagaattgagagacggaaatgcacggtgtttccattccacccgcaagaggcgaaagaagagcgtagtagaaagc acggagttgtggtttggatcccaagcaatctcgagaaactcatagtaaccgctgcgaaagagctagggctatcggatggagcctcatt tgtactattatccgaagaccaaggtcgtatcacagacattgatatgattagtgatggacacaaattgtatatgatcagtgatactactgat caaaca SEQ ID NO: 30 PN MGRLRRRQEIIDHEEEESNDDVSSDDGDLSLAETFDWLDSSEDDDIETDGDNDYDYIIDPKNR WYKAWEMFILVWAIYSSLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQTYRT VYKPTRIAFRYLKSHFLMDFIGCFPWDLIYKASGKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRI NYLFTRILKLLFVEVYCTHTAACIFYYLATTLPPENEGYTWIGSLKLGDYSYENFREIDLWKRYTT ALYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNITALIVKGSNTERFRDKMNDLI SFMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCST 14051746-1 EFINQIVIRLHEEYFLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISI ICNISQPFTVRVCELCHLLRLDKQSFSNILEIYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQ EAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAACRGYEDITLFLIQEGVDVN LKDKFGHTPLFEAVKAGQEGVIGLLAKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGMDP NSEDYDHRTPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDTK NAQSSIYPTSLRELQEERIERRKCTVFPFHPQEAKEERSRKHGVVVWIPSNLEKLIVTAAKELGL SDGASFVLLSEDQGRITDIDMISDGHKLYMISDTTDQT SEQ ID NO: 31 G.max Voltage-gated potassium channel. GenBank: KAG4383022.1 MIGFIMTFNLKPRRRRRSIQENGNRSSNKLSPIINIFLLLLKMTGKKNVKAATTTTPEEEDQRKQTTTSS SPSSSSRSSSSSSSSDEREYEVQDLRDRLKSSRGSRFDLIENQLGLNSTWSKFSRQALLHGIRGFSVDFV IHPDNRWYRAWTKFILLWAVYSSFFTPMEFGFFRGLPENLFILDIIGQIAFLVDIVLQFFVAYRDSQTYR TVYKRTPIALRYLKSNFIFDLLGCMPWDIIYKACGRKEEVRYLLWIRLYRVRKVTDFFHKLEKDIRVNYI ITRIVKLIVVELYCTHTAACIFYYLATTLPESQEGYTWIGSLKLGDFSYSHFREIDLWKRYTTSLYFAIV TMATVGYGDIHAVNMREMVFIMVYVSFDMILGAYLIGNMTALIVKGSKTEKFRDKMTDLMKYMNRNRLGR DIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQTLYLPYIEKVSLFKGCSSEFIRQIVIRLHEEFF LPGEVIMEQGNVVDQLYFVCHGVLEEVGTAEDGTEETVSLLQPNSSFGEISILCNIPQPYTVRVCELSRL LRLDKQSFTNILDIYFYDGRKVLNNLLEGKESFRDKQLESDITFHIGKQEAELALKVNNAAFNGDLYQLK GLIRAGADPNKTDYDGRSPLHLAASRGYEDITLFLIQERVDVNIKDNFGNTPLLEAVKNGHDRVASLLVR EGASMKIENAGSFLCTAVARGDSDYLKRLLSNGMDPNLKDYDYRSPLHIAAAEGLYFMAKLLLEGGASVF TKDRWGNTPLDEARMCGNKNLIKLLEDAKSAQLSEFPSQEYTDKMHPKKCTVFPYHPWDPKDNRRHGIVL WIPHSIQELIKSAAEQIEFSGDACILSEDAGKVTDVDMIKDGQKLYLVHETH SEQ ID NO: 32 G.max Voltage-gated potassium channel. GenBank: KAG4402629.1. MTGKKNVKAMTTAEEEDDQGKHTTSSSFSSSSSPSSSSDEREYEVQDLRDRLKSSQGSMFNLIENQLGLN STWSKFSRQALLHGIRGFSMDLVKDFVIHPDNRWYRAWTNFILVWAVYSSFFTPMEFGFFRGLPENLFIL DIIGQIAFLVDIVLQFFVAYRDSQTYRMVYKRTPIALRYLKSNFIFDLLGCMPWDIIYKACGRKEEVRYL LWIRLYRVRKVEDFFHKLEKDIRVNYIITRIVKLIVVELYCTHTAACIFYYLATTLPESQEGYTWIGSLK LGDFSYSHFREIDLWKRYTTSLYFAIVTMATVGYGDMHAVNMREMIFIMVYVSFDMILGAYLIGNMTALI VKGSKTEKFRDKMTDLMKYMNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQTLYLPY IEKVSLFKGCSSEFINQIVIRLHEEFFLPGEVIMEQGNVVDQLYFEEVGIAEDGTEETVSLLQPNSSFGE ISILCNIPQPYTVRVCELGRLLRLDKQSFTNILDIYFYDGRKVLYNLLEGKESFRDKQLESDITFHLGKQ EAELALKVNSAAFNGDMYQLKGLIRAGADPNKADYDGRSPLHLAASRGYEDITIFLIQERVDVNIIDNFG NTPLLEAVKNGHDRVASLLVKEGASMKIENAGSFLCTAVARGDSDYLKRLLSNGMDPNLKDYDYRSPLHV AAAEGLYFMAKLLLEAGASVFTRDRWGNTPLDEARMCGNKNLIKLLEDAKSSQLSEFPSQEFTDKMHPKK CTVFPFHPWDPKDNRRHGIVLWIPHSIEELIKSAAEQIEISGGSCILSEDAGKITDVDMIKDGQKLYLVH ETH SEQ ID NO: 33 G.max Voltage-gated potassium channel. GenBank: KAG4402628.1. MTGKKNVKAMTTAEEEDDQGKHTTSSSFSSSSSPSSSSDEREYEVQDLRDRLKSSQGSMFNLIENQLGLN STWSKFSRQALLHGIRGFSMDLVKDFVIHPDNRWYRAWTNFILVWAVYSSFFTPMEFGFFRGLPENLFIL DIIGQIAFLVDIVLQFFVAYRDSQTYRMVYKRTPIALRYLKSNFIFDLLGCMPWDIIYKACGRKEEVRYL LWIRLYRVRKVEDFFHKLEKDIRVNYIITRIVKLIVVELYCTHTAACIFYYLATTLPESQEGYTWIGSLK LGDFSYSHFREIDLWKRYTTSLYFAIVTMATVGYGDMHAVNMREMIFIMVYVSFDMILGAYLIGNMTALI VKGSKTEKFRDKMTDLMKYMNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQTLYLPY IEKVSLFKGCSSEFINQIEEVGIAEDGTEETVSLLQPNSSFGEISILCNIPQPYTVRVCELGRLLRLDKQ SFTNILDIYFYDGRKVLYNLLEGKESFRDKQLESDITFHLGKQEAELALKVNSAAFNGDMYQLKGLIRAG ADPNKADYDGRSPLHLAASRGYEDITIFLIQERVDVNIIDNFGNTPLLEAVKNGHDRVASLLVKEGASMK IENAGSFLCTAVARGDSDYLKRLLSNGMDPNLKDYDYRSPLHVAAAEGLYFMAKLLLEAGASVFTRDRWG NTPLDEARMCGNKNLIKLLEDAKSSQLSEFPSQEFTDKMHPKKCTVFPFHPWDPKDNRRHGIVLWIPHSI EELIKSAAEQIEISGGSCILSEDAGKITDVDMIKDGQKLYLVHETH 14051746-1 SEQ ID NO: 34 Z.mays KOR1 channel. GenBank: PWZ19722.1. MVRGLGSKRRVAEEESSEEEYEVEVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFF HGLVIHPDNKWYRLWTKFILVWAVYSSFFTPLEFGFFRGLPKNLFFLDVAGQTAFLIDIVVRFFVAYRDP DTYRVVYSPTAIALRYCKSSFVFDLLGCLPWDAIYKACGSKEEVRYLLWIRLTRVTKVTEFFWRLEKDIR VNYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGHTWIGSLQLGDYRFTHFREIDLAKRYITSLY FAIVTMATVGYGDIHAVNIREMIFIMIYVSFDMILGAYLIGNMTALIVKGSRTERFRDKMKEVIRYMNRN KLGKEIREQIKGHLRLQYESSYTEASVLQDIPISIRAKISQTLYKPYIESIPLFKGCSAEFIQQIVIRLQ EEFFLPGEVILEQGSAVDQLYFVCHGALEGVGIGEDGQEETLLMLEPESSFGEISILCNIPQPYTVRVCE LCRLLRLDKQSFTNILEIYFVDGRRILSNLSESEYGGRVKQLESDITFHIGKQEAELTLRVNSAAFYGDL HQLKSLIRAGADPKNTDYDGRSPLHLAASRGYEDVVQFLINEGVDIDLTDQFGNTPLLEAVKQGHERVAA LLFAKGAKLSLKNAGSHLCTAVAKGDSDFIRRALAYGADPNCRDYDHRTPLHVAAAEGLYLIAKMLVEAG ASVFTTDRWGTTPLDEARKCGGRTLGALLEEARASELSMFPERGEEVRDKVHPRRCSVFPYHPWRASAGE ERRAEGVVLWIPHTIESLVASAQEKLGLPGPAASRLRLLCEDGARVLDVDMVNDGQKLYLVGGEDGDQED GQ SEQ ID NO: 35 Z.mays Voltage-gated potassium channel. GenBank: AAW82753.1 AEGFLHDLVIHPDNKWYRLWTKFILVWAVYSSFFTPLEFGFFRGLPKNLFFLDVAGQTAFLIDIVVRFFV AYRDPDTYRVVYSPTAIALRYCKSSFVFDLLGCLPWDAIYKACGSKEEVRYLLWIRLTRVTKVTEFFWRL EKDIRVNYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGHTWIGSLQLGDYRFTHFREIDLAKRY ITSLYFAIVTMATVGYGDIHAVNIREMIFIMIYVSFDMILGAYLIGNMTALIVKGSRTERFRDKVKEVIR YMNRNKLGKEIREQIKGHLRLQYESNYTEASVLQDIPISIRAKISQTLYKPYIESIPLFKGCSAEFIQQI VIRLQEEFFLPGEVILEQGSAVDQLYFVCHGALEGVGIGEDGQEETLLMLEPESSFGEISILCNIPQPYT VRVCELCRLLRLDKQSFTNILEIYFVDGRRILSNLSESEYGGRVKQLESDITFHIGKQEAELTLRVNSAA FYGDLHQLKSLIRAGADPKNTDYDDRSPLHLAASRGYEDVVQFLINEGVDVDLTDQFGNTPLLEAVKQGH ERVAALLFAKGAKLSLKNAGSHLCTAVAKGDSDLIRRALAYGADPNCRDCDHRTPLHIAAAEGLYLIAKM LVEAGASVFTTDRWGTTPLDEARKCGGRTLGALLEEARASELSMFPERGEEVRDKVHPRRCSVFPYHPWR ASAGEERRAEGVVLWIPHTIESLVASAQEKLGLPGPAASRLRLLCEDGARVLDVDMVNDGQKLYLVGGED GDQKYGQ SEQ ID NO: 36 Z.mays SKOR. GenBank: AQK83496.1 MVRGLGSKRRVAEEESSEEEYEVEVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFF HGLVIHPDNKWYRLWTKFILVWAVYSSFFTPLEFGFFRGLPKNLFFLDVAGQTAFLIDIVVRFFVAYRDP DTYRVVYSPAAIALRYCKSSFVFDLLGCLPWDAIYKACGSKEEVRYLLWIRLTRVTKVTEFFWRLEKDIR VNYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGHTWIGSLQLGDYRFTHFREIDLAKRYITSLY FAIVTMATVGYGDIHAVNIREMIFIMIYVSFDMILGAYLIGNMTALIVKGSRTERFRDKMKEVIRYMNRN KLGKEIREQIKGHLRLQYESSYTEASVLQDIPISIRAKISQTLYKPYIESIPLFKGCSAEFIQQIVIRLQ EEFFLPGEVILEQGSAVDQLYFVCHGALEGVGIGEDGQEETLLMLEPESSFGEISILCNIPQPYTVRVCE LCRLLRLDKQSFTNILEIYFVDGRRILSNLSESEYGGRVKQLESDITFHIGKQEAELTLRVNSAAFYGDL HQLKSLIRAGADPKNTDYDGRSPLHLAASRGYEDVVQFLINEGVDIDLTDQFGNTPLLEAVKQGHERVAA LLFAKGAKLSLKNAGSHLCTAVAKGDSDFIRRALAYGADPNCRDYDHRTPLHIAAAEGLYLIAKMLVEAG ASVFTTDRWGTTPLDEARKCGGRTLGALLEEARASELSMFPERGEEVRDKVHPRRCSVFPYHPWRASAGE ERRAEGVVLWIPHTIESLVASAQEKLGLPGPAASRLRLLCEDGARVLDVDMVNDGQKLYLVGGEDGDQEG VEENVIKSIIRAGHCTELQIGNNVRCEMKMQC A’ Helix SEQ ID NO: 37. A’ helix domain of the C-linker of A. thaliana GORK. VKGSNTERFRDKMNDLISFMNRKK SEQ ID NO: 38. A’ helix domain of the C-linker of G.max SKOR and the voltage-gated potassium channels KAG4383022.1 and KAG4402629.1 and KAG4402628.1 VKGSKTEKFRDKMTDLMKYMNRNR SEQ ID NO: 39. A’ helix domain of the C-linker of Z.mays KOR1 and SKOR and the voltage- gated potassium channel AAW82753.1 14051746-1 VKGSRTERFRDKMKEVIRYMNRNK B’ Helix SEQ ID NO: 40. B’ helix domain of the C-linker of A. thaliana GORK. RDLRSQITGHVRLQYDS SEQ ID NO: 41. B’ helix domain of the C-linker of the G.max SKOR and the voltage-gated potassium channels KAG4383022.1 and KAG4402629.1 and KAG4402628.1 RDIREQIKGHVRLQYES SEQ ID NO: 42. B’ helix domain of the C-linker of Z.mays KOR1 and SKOR and the voltage- gated potassium channel AAW82753.1 KEIREQIKGHLRLQYES C’ Helix SEQ ID NO: 43. B’ helix domain of the C-linker of A. thaliana GORK. TDTVMLQD SEQ ID NO: 44. B’ helix domain of the C-linker of the G.max SKOR and the voltage-gated potassium channels KAG4383022.1 and KAG4402629.1 and KAG4402628.1 TEASVIQDI SEQ ID NO: 45. B’ helix domain of the C-linker of Z.mays KOR1 and SKOR and the voltage- gated potassium channel AAW82753.1 TEASVIQDI D’ Helix SEQ ID NO: 46. B’ helix domain of the C-linker of A. thaliana GORK. PASIRAKIAQLLYLPYIKKVPLF SEQ ID NO: 47. B’ helix domain of the C-linker of the G.max SKOR and the voltage-gated potassium channels KAG4383022.1 and KAG4402629.1 and KAG4402628.1 PISIRAKISQTLYLPYIEKVSLF SEQ ID NO: 48. B’ helix domain of the C-linker of Z.mays KOR1 and SKOR and the voltage- gated potassium channel AAW82753.1 PISIRAKISQTLYKPYIESIPLF Mutated C-linker SEQ ID NO: 49. A.thaliana. K312A, E317A, D321A MGRLRRRQEIIDHEEEESNDDVSSRRGKLSLAETFRWLDSSEHRRIETDGHNDYKYIIHPKNRWYKAWEMFILVWAIYS SLFTPMEFGFFRGLPERLFVLDIVGQIAFLVDIVLQFFVAYRDTQSYRTVYKPTRIAFRYLKSHFLMDFIGCFPWDLIYKAS GKHELVRYLLWIRLFRVRKVVEFFQRLEKDTRINYLFTRILKLLFVEVYCTHTAACIFYYLATTLPPEQEGYTWIGSLKLGDY SYENFREIDLWKRYTTALYFAIVTMATVGYGDIHAVNLREMIFVMIYVSFDMVLGAYLIGNVTALIVAGSNTARFRAKM NDLISFMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQLLYLPYIKKVPLFKGCSTEFINQIVIRLHEEY FLPGEVITEQGNVVDHLYFVCEGLLEALVTKTDGSEESVTLLGPHTSFGDISIICNISQPFTVRVCELCHLLRLDKQSFSNILE IYFHDGRTILNNIMEEKESNDRIKKLESDIVIHIGKQEAELALKVNSAAFQGDFYQLKSLIRSGADPNKTDYDGRSPLHLAA CRGYEDITLFLIQEGVDVNLKDKFGHTPLFEAVKAGQEGVIGLLVKEGASFNLEDSGNFLCTTVAKGDSDFLKRLLSSGM NPNSEDYDHRTPLHVAASEGLFLMAKMLVEAGASVISKDRWGNSPLDEARLCGNKKLIKLLEDVKNAQSSIYPSSLREL QEERIERRKCTVFPFHPQEAKEERSRKHGVVVWVPSNLEKLIVTAAKELGLSDGASFVLLSEDQGRITDIDMISDGHKLY MISDTTDQT 14051746-1 SEQ ID NO: 50. G.max Voltage-gated potassium channel. K395A, E400A, D404A MIGFIMTFNLKPRRRRRSIQENGNRSSNKLSPIINIFLLLLKMTGKKNVKAATTTTPEEEDQRKQTTTSS SPSSSSRSSSSSSSSDEREYEVQDLRDRLKSSRGSRFDLIENQLGLNSTWSKFSRQALLHGIRGFSVDFV IHPDNRWYRAWTKFILLWAVYSSFFTPMEFGFFRGLPENLFILDIIGQIAFLVDIVLQFFVAYRDSQTYR TVYKRTPIALRYLKSNFIFDLLGCMPWDIIYKACGRKEEVRYLLWIRLYRVRKVTDFFHKLEKDIRVNYI ITRIVKLIVVELYCTHTAACIFYYLATTLPESQEGYTWIGSLKLGDFSYSHFREIDLWKRYTTSLYFAIV TMATVGYGDIHAVNMREMVFIMVYVSFDMILGAYLIGNMTALIVAGSKTAKFRAKMTDLMKYMNRNRLGR DIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQTLYLPYIEKVSLFKGCSSEFIRQIVIRLHEEFF LPGEVIMEQGNVVDQLYFVCHGVLEEVGTAEDGTEETVSLLQPNSSFGEISILCNIPQPYTVRVCELSRL LRLDKQSFTNILDIYFYDGRKVLNNLLEGKESFRDKQLESDITFHIGKQEAELALKVNNAAFNGDLYQLK GLIRAGADPNKTDYDGRSPLHLAASRGYEDITLFLIQERVDVNIKDNFGNTPLLEAVKNGHDRVASLLVR EGASMKIENAGSFLCTAVARGDSDYLKRLLSNGMDPNLKDYDYRSPLHIAAAEGLYFMAKLLLEGGASVF TKDRWGNTPLDEARMCGNKNLIKLLEDAKSAQLSEFPSQEYTDKMHPKKCTVFPYHPWDPKDNRRHGIVL WIPHSIQELIKSAAEQIEFSGDACILSEDAGKVTDVDMIKDGQKLYLVHETH SEQ ID NO: 51 >Glycine max SKOR K353A, E358A, D362A MTGKKNVKAATTTTPEEEDQRKQTTTSSSPSSSSRSSSSSSSSDEREYEVQDLRDRLKSSRGSRFDLIENQLGLNSTWSKF SRQALLHGIRGFSVDFVIHPDNRWYRAWTKFILLWAVYSSFFTPMEFGFFRGLPENLFILDIIGQIAFLVDIVLQFFVAYRD SQTYRTVYKRTPIALRYLKSNFIFDLLGCMPWDIIYKACGRKEEVRYLLWIRLYRVRKVTDFFHKLEKDIRVNYIITRIVKLIV VELYCTHTAACIFYYLATTLPESQEGYTWIGSLKLGDFSYSHFREIDLWKRYTTSLYFAIVTMATVGYGDIHAVNMREMV FIMVYVSFDMILGAYLIGNMTALIVAGSKTAKFRAKMTDLMKYMNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPI SIRAKISQTLYLPYIEKVSLFKGCSSEFIRQIVIRLHEEFFLPGEVIMEQGNVVDQLYFVCHGVLEEVGTAEDGTEETVSLLQ PNSSFGEISILCNIPQPYTVRVCELSRLLRLDKQSFTNILDIYFYDGRKVLNNLLEGKESFRDKQLESDITFHIGKQEAELALK VNNAAFNGDLYQLKGLIRAGADPNKTDYDGRSPLHLAASRGYEDITLFLIQERVDVNIKDNFGNTPLLEAVKNGHDRVA SLLVREGASMKIENAGSFLCTAVARGDSDYLKRLLSNGMDPNLKDYDYRSPLHIAAAEGLYFMAKLLLEGGASVFTKDR WGNTPLDEARMCGNKNLIKLLEDAKSAQLSEFPSQEYTDKMHPKKCTVFPYHPWDPKDNRRHGIVLWIPHSIQELIKS AAEQIEFSGDACILSEDAGKVTDVDMIKDGQKLYLVHETH SEQ ID NO: 52 Z.mays KOR1 channel. K329A, E334A, D338A MVRGLGSKRRVAEEESSEEEYEVEVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFF HGLVIHPDNKWYRLWTKFILVWAVYSSFFTPLEFGFFRGLPKNLFFLDVAGQTAFLIDIVVRFFVAYRDP DTYRVVYSPTAIALRYCKSSFVFDLLGCLPWDAIYKACGSKEEVRYLLWIRLTRVTKVTEFFWRLEKDIR VNYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGHTWIGSLQLGDYRFTHFREIDLAKRYITSLY FAIVTMATVGYGDIHAVNIREMIFIMIYVSFDMILGAYLIGNMTALIVAGSRTARFRAKMKEVIRYMNRN KLGKEIREQIKGHLRLQYESSYTEASVLQDIPISIRAKISQTLYKPYIESIPLFKGCSAEFIQQIVIRLQ EEFFLPGEVILEQGSAVDQLYFVCHGALEGVGIGEDGQEETLLMLEPESSFGEISILCNIPQPYTVRVCE LCRLLRLDKQSFTNILEIYFVDGRRILSNLSESEYGGRVKQLESDITFHIGKQEAELTLRVNSAAFYGDL HQLKSLIRAGADPKNTDYDGRSPLHLAASRGYEDVVQFLINEGVDIDLTDQFGNTPLLEAVKQGHERVAA LLFAKGAKLSLKNAGSHLCTAVAKGDSDFIRRALAYGADPNCRDYDHRTPLHVAAAEGLYLIAKMLVEAG ASVFTTDRWGTTPLDEARKCGGRTLGALLEEARASELSMFPERGEEVRDKVHPRRCSVFPYHPWRASAGE ERRAEGVVLWIPHTIESLVASAQEKLGLPGPAASRLRLLCEDGARVLDVDMVNDGQKLYLVGGEDGDQED GQ SEQ ID NO: 53 Z.mays Voltage-gated potassium channel. GenBank: AAW82753.1 AEGFLHDLVIHPDNKWYRLWTKFILVWAVYSSFFTPLEFGFFRGLPKNLFFLDVAGQTAFLIDIVVRFFV AYRDPDTYRVVYSPTAIALRYCKSSFVFDLLGCLPWDAIYKACGSKEEVRYLLWIRLTRVTKVTEFFWRL EKDIRVNYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGHTWIGSLQLGDYRFTHFREIDLAKRY ITSLYFAIVTMATVGYGDIHAVNIREMIFIMIYVSFDMILGAYLIGNMTALIVAGSRTARFRAKVKEVIR YMNRNKLGKEIREQIKGHLRLQYESNYTEASVLQDIPISIRAKISQTLYKPYIESIPLFKGCSAEFIQQI VIRLQEEFFLPGEVILEQGSAVDQLYFVCHGALEGVGIGEDGQEETLLMLEPESSFGEISILCNIPQPYT VRVCELCRLLRLDKQSFTNILEIYFVDGRRILSNLSESEYGGRVKQLESDITFHIGKQEAELTLRVNSAA FYGDLHQLKSLIRAGADPKNTDYDDRSPLHLAASRGYEDVVQFLINEGVDVDLTDQFGNTPLLEAVKQGH ERVAALLFAKGAKLSLKNAGSHLCTAVAKGDSDLIRRALAYGADPNCRDCDHRTPLHIAAAEGLYLIAKM LVEAGASVFTTDRWGTTPLDEARKCGGRTLGALLEEARASELSMFPERGEEVRDKVHPRRCSVFPYHPWR ASAGEERRAEGVVLWIPHTIESLVASAQEKLGLPGPAASRLRLLCEDGARVLDVDMVNDGQKLYLVGGED GDQKYGQ 14051746-1 SEQ ID NO: 54 Z.mays SKOR channel. K329A, E334A, D338A MVRGLGSKRRVAEEESSEEEYEVEVVRDHIASSRGSRLALFGSELRLGRFRPRRRRRLPLAGEGAAEGFF HGLVIHPDNKWYRLWTKFILVWAVYSSFFTPLEFGFFRGLPKNLFFLDVAGQTAFLIDIVVRFFVAYRDP DTYRVVYSPAAIALRYCKSSFVFDLLGCLPWDAIYKACGSKEEVRYLLWIRLTRVTKVTEFFWRLEKDIR VNYLFTRIVKLIVVELYCTHTAACIFYYLATTLPESMEGHTWIGSLQLGDYRFTHFREIDLAKRYITSLY FAIVTMATVGYGDIHAVNIREMIFIMIYVSFDMILGAYLIGNMTALIVAGSRTARFRAKMKEVIRYMNRN KLGKEIREQIKGHLRLQYESSYTEASVLQDIPISIRAKISQTLYKPYIESIPLFKGCSAEFIQQIVIRLQ EEFFLPGEVILEQGSAVDQLYFVCHGALEGVGIGEDGQEETLLMLEPESSFGEISILCNIPQPYTVRVCE LCRLLRLDKQSFTNILEIYFVDGRRILSNLSESEYGGRVKQLESDITFHIGKQEAELTLRVNSAAFYGDL HQLKSLIRAGADPKNTDYDGRSPLHLAASRGYEDVVQFLINEGVDIDLTDQFGNTPLLEAVKQGHERVAA LLFAKGAKLSLKNAGSHLCTAVAKGDSDFIRRALAYGADPNCRDYDHRTPLHIAAAEGLYLIAKMLVEAG ASVFTTDRWGTTPLDEARKCGGRTLGALLEEARASELSMFPERGEEVRDKVHPRRCSVFPYHPWRASAGE ERRAEGVVLWIPHTIESLVASAQEKLGLPGPAASRLRLLCEDGARVLDVDMVNDGQKLYLVGGEDGDQEG VEENVIKSIIRAGHCTELQIGNNVRCEMKMQC SEQ ID NO: 55. GORK N-terminal domain DDVSSRRGKLSLAETFRWLDSSEHRRIETDGHNDYKYIIHPKNRWYK SEQ ID NO: 56. A. thaliana GORK C-linker VKGSNTERFRDKMNDLISFMNRKKLGRDLRSQITGHVRLQYDSHYTDTVMLQDIPASIRAKIAQ LLYLPYIKKVPLF SEQ ID NO: 57. G.max voltage-gated potassium channel C-linker VKGSKTEKFRDKMTDLMKYMNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQT LYLPYIEKVSLF SEQ ID NO: 58. G.max voltage-gated potassium channel C-linker VKGSKTEKFRDKMTDLMKYMNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQT LYLPYIEKVSLF SEQ ID NO: 59. G.max SKOR channel C-linker VKGSKTEKFRDKMTDLMKYMNRNRLGRDIREQIKGHVRLQYESSYTEASVIQDIPISIRAKISQT LYLPYIEKVSLF SEQ ID NO: 60. Z.mays KOR1 channel C-linker VKGSRTERFRDKMKEVIRYMNRNKLGKEIREQIKGHLRLQYESSYTEASVLQDIPISIRAKISQTL YKPYIESIPLF SEQ ID NO: 61. Z.mays voltage-gated potassium channel C-linker VKGSRTERFRDKVKEVIRYMNRNKLGKEIREQIKGHLRLQYESNYTEASVLQDIPISIRAKISQTL YKPYIESIPLF SEQ ID NO: 62. Z.mays SKOR channel C-linker VKGSRTERFRDKMKEVIRYMNRNKLGKEIREQIKGHLRLQYESSYTEASVLQDIPISIRAKISQTL YKPYIESIPLF SEQ ID NO: 77: KAT1 IDTIKQSSFLSADLLPSLGARINQSTKLRKHIISPFNPYRY SEQ ID NO: 78 gVSDa DDVSSAAGALSLAATFDWLDSSAAAAIATAGANAYAYIIAPKNRWYK SEQ ID NO: 79 gVSDa DDVSSDDGDLSLAETFDWLKSSKDDDIKTKGDNKYDYIIDPKNRWYK 14051746-1

Claims

CLAIMS:

1. A genetically altered plant, plant part or plant cell, wherein the plant is characterised by at least one mutation in a C-linker domain of a stomatal voltage- gated potassium channel, wherein the mutation is not a substitution of glycine at position 313 at SEQ ID NO:

1.

2. The genetically altered plant, plant part or plant cell of claim 1, wherein the C- linker domain comprises at least four alpha-helices, and wherein the at least one mutation is in the first N-terminal alpha helix, the second N-terminal helix or between the first and second alpha helices.

3. The genetically altered plant, plant part or plant cell of claim 2, wherein the first N-terminal alpha helix comprises a sequence selected from SEQ ID NO: 37 to 39, or a functional variant thereof, wherein the functional variant has at least 60% overall sequence identity to SEQ ID NO: 37 to 39.

4. The genetically altered plant, plant part or plant cell of claim 2, wherein the second N-terminal alpha helix comprises a sequence selected from SEQ ID NO: 40 to 42, or a functional variant thereof, wherein the functional variant has at least 60% identity to SEQ ID NO: 40 to 42.

5. The genetically altered plant, plant part or plant cell of claim 1, wherein the C- terminal helix comprises a (K / R)LGR domain, wherein the at least one mutation is within the (K / R)LGR domain.

6. The genetically altered plant, plant part or plant cell of any preceding claim, wherein the mutation is a substitution of at least one positively charged amino acid for a negatively charged amino acid or a neutral amino acid and / or, wherein the mutation is a substitution of at least one negatively charged amino acid for a positively charged amino acid or a neutral amino acid and / or wherein the mutation is the substitution of a neutral amino acid for a charged (positive or negative) or a residue with a larger mass.

7. The genetically altered plant, plant part or plant cell of any preceding claim, wherein the mutation is at a position selected from at least one of 312, 316, 317, 318, 319, 320, 321, 332, 333, 334, 335, 336, 337, 348, 349, 350, 351, 352 and / or 356 of SEQ ID NO: 1, or corresponding position in a homologous sequence, and wherein the mutation is not at position 313 of SEQ ID NO:

1.

8. The genetically altered plant, plant part or plant cell of claim 7, wherein the corresponding position in a homologous sequence is selected from: 14051746-1a. positions 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434 and 435 of SEQ ID NO: 31; or b. positions 352, 356, 357, 358, 359, 360, 361, 372, 373, 374, 375, 376, 377, 388, 389, 390, 391 and 392 of SEQ ID NO: 32 or 33; or c. positions 353, 357, 358, 359, 360, 361, 362, 373, 374, 375, 376, 377, 378, 389, 390, 391, 392 and 393 of SEQ ID NO:

17.

9. The genetically altered plant, plant part or plant cell of claim 7, wherein the corresponding position in a homologous sequence is selected from: a. positions 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434 and 435 of SEQ ID NO: 34 or 36; or b. positions 264, 268, 269, 270, 271, 272, 273, 284, 285, 286, 287, 288, 289, 300, 301, 302, 303 and 304 of SEQ ID NO:

35.

10. The genetically altered plant, plant part or plant cell of claim 7, wherein the mutation is at least two mutations at positions selected from K312, E317, D321 of SEQ ID NO: 1 or at least two corresponding positions in a homologous sequence.

11. The genetically altered plant, plant part or plant cell of claim 10, wherein the at least two corresponding positions of a homologous sequence are selected from: a. K395, E400 and D404 of SEQ ID NO: 31; or b. K352, E357 and D361 of SEQ ID NO: 32 or 33; or c. K353, E358 and D362 of SEQ ID NO:

17.

12. The genetically altered plant, plant part or plant cell of claim 10, wherein the at least two corresponding positions of a homologous sequence are selected from: a. K329, E334 and D338 of SEQ ID NO: 34 or 36; or b. K264, E269 and D273 of SEQ ID NO:

35.

13. The genetically altered plant, plant part or plant cell of any preceding claim, wherein the plant, part thereof or plant cell further comprises at least one mutation in a N-terminal cytosolic domain.

14. The genetically altered plant, plant part or plant cell of claim 13, wherein the at least one mutation alters the pattern of charged amino acids in the N-terminal domain.

15. The genetically altered plant, plant part or plant cell of claim 14, wherein the mutation is the substitution of at least one positively charged amino acid for a negatively charged amino acid or a neutral amino acid and / or wherein the 14051746-1mutation is the substitution of at least one negatively charged amino acid for a positively charged amino acid or a neutral amino acid.

16. The genetically altered plant, plant part or plant cell of claim 13, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal domain.

17. A genetically altered plant, plant part or plant cell, wherein the plant is characterised by at least one mutation in a N-terminal cytosolic domain of a stomatal voltage-gated potassium channel, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal.

18. The genetically altered plant, plant part or plant cell of any claim 17, wherein the N-terminal domain comprises SEQ ID NO: 55 or a variant thereof.

19. The genetically altered plant, plant part or plant cell of any preceding claim, wherein the stomatal voltage-gated potassium channel is a GORK channel.

20. The genetically altered plant, plant part or plant cell of claim any preceding claim, wherein the GORK channel comprises an amino acid sequence as defined in SEQ ID NO: 1, 3, 5 or a functional variant or homologue thereof.

21. The genetically altered plant, plant part or plant cell of any preceding claim, wherein the plant is a monocot or dicot.

22. The genetically altered plant part of any preceding claim, wherein the plant part is a seed.

23. A method of altering the channel kinetics of a stomatal voltage-gated potassium channel, wherein an alteration in channel kinetics is preferably selected from a change in sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage-sensitive ion channel (I), wherein the method comprises introducing at least one mutation into the C- linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is not a mutation at position 313 of SEQ ID NO: 1 and / or or at least one mutation into the cytosolic N-terminal domain, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N- terminal.

24. A method of increasing at least one of growth, yield, drought tolerance, water use efficiency and / or carbon assimilation in a plant, wherein the method comprises 14051746-1introducing at least one mutation into the C-linker domain of a stomatal voltage- gated potassium channel, wherein the mutation is not a mutation at position 313 of SEQ ID NO: 1 and / or or at least one mutation into the cytosolic N-terminal domain, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal.

25. A method of producing a genetically altered plant, part thereof or plant seed, the method comprising introducing at least one mutation into the C-linker domain of a stomatal voltage-gated potassium channel, wherein the mutation is not a mutation at position 313 of SEQ ID NO: 1 and / or or at least one mutation into the cytosolic N-terminal domain, wherein the mutation is the deletion of residues 2 to 60, preferably 2-50, preferably 2-32, preferably 2-23, preferably 2-12 and even more preferably residues 2 to 7 of the cytosolic N-terminal.

26. The method of any of claims 23 to 25, wherein the C-linker domain comprises at least four alpha-helices, and wherein the at least one mutation is in the first N- terminal alpha helix, the second N-terminal helix or between the first and second alpha helices.

27. The method of claim 26, wherein the first N-terminal alpha helix comprises a sequence selected from SEQ ID NO: 37 to 39, or a functional variant thereof.

28. The method of claim 26, wherein the second N-terminal alpha helix comprises a sequence selected from SEQ ID NO: 40 to 42, or a functional variant thereof.

29. The method of claim 26, wherein the C-terminal helix comprises a (K / R)LGR domain, and the at least one mutation is within the (K / R)LGR domain.

30. The method of any of claims 23 to 29, wherein the mutation is a substitution of at least one positively charged amino acid for a negatively charged amino acid or a neutral amino acid and / or wherein the mutation is a substitution of at least one negatively charged amino acid for a positively charged amino acid or a neutral amino acid and / or wherein the mutation is the substitution of a neutral amino acid for a charged (positive or negative) or a residue with a larger mass.

31. The method of claim any of claims 23 to 29, wherein the mutation is at a position selected from at least one of 312, 316, 317, 318, 319, 320, 321, 332, 333, 334, 335, 336, 337, 348, 349, 350, 351, 352 and / or 356 of SEQ ID NO: 1, or corresponding position in a homologous sequence, and wherein the mutation is not at position 313 of SEQ ID NO:

1. 14051746-132. The method of claim 31, wherein the corresponding position in a homologous sequence is selected from: a. positions 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434 and 435 of SEQ ID NO: 31; or b. positions 352, 356, 357, 358, 359, 360, 361, 372, 373, 374, 375, 376, 377, 388, 389, 390, 391 and 392 of SEQ ID NO: 32 or 33; or c. positions 353, 357, 358, 359, 360, 361, 362, 373, 374, 375, 376, 377, 378, 389, 390, 391, 392 and 393 of SEQ ID NO:

17.

33. The method of claim 31, wherein the corresponding position in a homologous sequence is selected from: a. Positions 395, 399, 400, 401, 402, 403, 404, 415, 416, 417, 418, 419, 420, 431, 432, 433, 434 and 435 of SEQ ID NO: 34 or 36; or b. positions 264, 268, 269, 270, 271, 272, 273, 284, 285, 286, 287, 288, 289, 300, 301, 302, 303 and 304 of SEQ ID NO:

35.

34. The method of claim 31, wherein the mutation is at least two mutations at positions selected from K312, E317, D321 of SEQ ID NO: 1 or at least two corresponding positions in a homologous sequence.

35. The method of claim 34, wherein the at least two corresponding positions of a homologous sequence are selected from: a. K395, E400 and D404 of SEQ ID NO: 31; or b. K352, E357 and D361 of SEQ ID NO: 32 or 33; or c. K353, E358 and D362 of SEQ ID NO:

17.

36. The method of claim 34, wherein the at least two corresponding positions of a homologous sequence are selected from a. K329, E334 and D338 of SEQ ID NO: 34 or 36; or b. K264, E269 and D273 of SEQ ID NO:

35.

37. The method of any of claims 23 to 36, wherein the plant, part thereof or plant cell further comprises at least one mutation in a N-terminal cytosolic domain.

38. The method of claim 37, wherein the at least one mutation alters the pattern of charged amino acids in the N-terminal domain.

39. The method of claim 38, wherein the mutation is the substitution of at least one positively charged amino acid for a negatively charged amino acid or a neutral amino acid and / or wherein the mutation is the substitution of at least one negatively charged amino acid for a positively charged amino acid or a neutral amino acid. 14051746-140. A nucleic acid construct comprising a nucleic acid sequence encoding a voltage- gated potassium channel comprising at least one mutation in the C-linker domain, wherein the at least one mutation is not at position 313 of SEQ ID NO:

1.

41. The nucleic acid construct of claim 40, wherein the nucleic acid construct comprises a nucleic acid sequence encoding a voltage-gated potassium channel selected from SEQ ID NO: 49, 50, 51, 52, 53 and 54 or a functional variant thereof, wherein the functional variant has at least 60% overall sequence identity to one of SEQ ID NO: 49, 50, 51, 52, 53 and 54, wherein preferably the nucleic acid sequence encoding a voltage-gated potassium channel is operably linked to a regulatory sequence.

42. An isolated plant cell transfected with at least one nucleic acid construct as defined in any of claims 40 to 41.

43. The use of a nucleic acid construct as defined in any of claims 40 to 42 to increase at least one of growth, yield, drought tolerance, water use efficiency and / or carbon assimilation in a plant.

44. A method of screening a population of plants and identifying and / or selecting a plant that has an alteration in channel kinetics of a stomatal voltage-gated potassium channel, wherein an alteration in channel kinetics is preferably selected from a change in sensitivity of the gate to a change in voltage (V1 / 2), maximum ensemble conductance (Gmax) and / or ensemble current of a voltage- sensitive potassium channel (I) in a plant compared to a control or wild-type plant, the method comprising detecting at least one polymorphism or mutation in the N-terminal domain or C-linker domain or in both the N-terminal and C-linker domains of a voltage-gated potassium channel gene, wherein said polymorphism or mutation leads to an alteration in the channel kinetics of the stomatal voltage- gated potassium channel.

45. The method of claim 44, wherein the voltage-gated potassium channel is selected from GORK, SKOR or KOR.

46. The method of claim 44 or 45, wherein the plant is further characterised by an altered rate of stomatal closure, yield, increased water use efficiency and / or increased carbon assimilation. 14051746-1

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