RUST RESISTANCE GENE.

Abstract

The present invention relates to a plant that has integrated into its genome an exogenous polynucleotide that encodes a polypeptide that confers resistance to at least one strain of Puccinia graminis.

Description

FIELD OF INVENTION The present invention relates to a plant that has integrated into its genome an exogenous polynucleotide that encodes a polypeptide that confers resistance to at least one strain of Puccinia graminis. BACKGROUND OF THE INVENTION Stem rust, caused by the fungal pathogen Puccinia graminis, has a long history of devastating cereal crop destruction and was documented as far back as Roman times. Yield losses in wheat due to stem rust Puccinia graminis f.sp. tritici (Pgt) have been reported in almost all major wheat-producing regions worldwide. The successful use of the 1B / 1R translocation resistance gene Sr31 in many high-yielding, CIMMYT-derived semidwarf cultivars during the well-known “Green Revolution” initiated by Dr. Norman Borlaug reduced the incidence of stem rust worldwide for almost 40 years. That was until the emergence of Ug99, a stem rust pathotype first identified in Uganda in 1999 that was reported to be virulent to Sr31 (Pretorius et al., 2000). Since then, numerous efforts have been made to search for Ug99 resistance genes (Singh et al., 2015). As a result, eight seedling R genes and two triple rust APR genes, namely Sr22, Sr33, Sr35, Sr45, Sr50, Sr13b, Sr21, Sr46, Lr34 / Yr18 / Sr57 and Lr67 / Yr46 / Sr56, were identified and successfully cloned as effective R genes against the Ug99 lineage (Saintenac et al., 2013; Mago et al., 2015; Zhang et al., 2017; Chen et al., 2018; Periyannan et al., 2013; Steuernagel et al., 2016; Krattinger et al., 2011; Moore et al., 2015). Recently, disease epidemics have been reported as a result of the re-emergence of the Digalu stem rust pathotype (TKTTF) in the UK after 60 years, rendering 80% of UK wheat cultivars susceptible. Furthermore, in 2017, Europe was reported to have experienced its most severe stem rust outbreaks in over 50 years, with vulnerable hosts expanding from wheat to barley. The causal pathotype of the Sicilian epidemic was initially thought to be the TTTTF race, a pathotype previously identified in Tanzania and Rwanda, but was later reconfirmed as TTRTF (Lewis et al., 2018; Bhattacharya et al., 2017). The significant pathogenicity difference between these two pathotypes is that TTRTF is virulent in Sr7a, Sr13b, Sr37, Sr44 and, most importantly, the newly cloned Ug99-resistant R genes Sr33 and Sr35.It is also reported that the TTRTF strain gives a high infection type in adult plants carrying the cloned Sr50 effective R gene derived from. QAfrQQn / 1 znz / q / YILI Secale cereale Ug99. In 2016, a report emerged of a new pathotype in Georgia, USA, which is virulent to Sr22, making the situation more urgent and demonstrating that the threat is not only from the Ug99 lineage. The story involving wheat R genes against mutant rust pathogen populations presents a recurring scenario. In some cases, even as scientists were celebrating the cloning of a new, unique R gene effective against a particular pathotype, the gene was later reported to be no longer fully effective due to the emergence of new, virulent pathotypes. Wheat relatives are a proven source of genetic resistance that can be transferred to commercial cultivars. The globally successful CIMMYT-derived wheats of the last century were protected by Sr2 (transferred from Triticum turgidum) and also Sr31 (from Petkus rye). The stem rust resistance locus Sr26 is derived from tall wheatgrass (Thinopyrum ponticum (Podp.) Barkworth & DR Dewey (Syn. Agropyron elongatum (Host.) Beauvoirssp. ruthenicum Beldie) (2n = 10x = 70)). Its introgression into wheat as the translocation of chromosome wheat-6Ae#1 has been considered one of the most successful examples of utilizing resistance resources from wheat wild relatives (Knott et al., 1961; Dundas et al., 2015). The Sr26 locus (Mclntosh et al., 1995) was transferred to chromosome 6A of wheat by Dr. Doug Knott of the University of Saskatchewan (Knott et al.Knott et al. (1961) used irradiation techniques, and it is a unique resistance that remains effective against all known Pgt pathotypes, including all races of the Ug99 group. Knott et al. (1961) used the wheat derivative Agropyron (now Thinopyrum) previously developed by L.H. Shebeski, and the translocation carrying Sr26 has been released in several Australian wheat cultivars (Park et al., 2009). McIntosh et al. (1995) made special mention of the fact that Sr26, along with Sr2, were two excellent examples of durable resistance to stem rust. It was proposed that this superior, durable resistance locus Sr26 was an integrated resistance effect due to a cluster of R loci in the introgressed Th. ponticum seed, similar to the case of Lr13 (Mundt, 2018). Molecular markers for Sr26 have been developed, but due to the presence of the Ph1 gene, which regulates chromosome pairing and recombination, there is no recombination between wheat and the introduced Th. ponticum chromosome segment. All markers developed so far for Sr26 are potentially physically distant from the gene and lack the specificity to reliably track the Sr26 gene itself. It is particularly difficult to differentiate Sr26 from other genes that also derive from the Th. ponticum origin. Consequently, it has not been possible to determine whether Sr26 resistance is a single locus or a cluster of resistance loci. QAfrQQn / L7n7 / 3 / YILI Therefore, there is a need to identify the Sr26 gene for use in the development of rust-resistant plants, such as cereal crops. SUMMARY OF THE INVENTION The present inventors have identified a new polypeptide and gene that confer a certain level of resistance to plants against Puccinia graminis. Therefore, in a first aspect, the present invention provides a plant comprising an exogenous polynucleotide encoding a polypeptide conferring resistance to at least one strain of Puccinia graminis, wherein the polypeptide comprises amino acids having a sequence as indicated in SEQ ID. NO:1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO:1. In one embodiment, the polynucleotide is operationally linked to a promoter capable of directing the expression of the polynucleotide in a plant cell. In another aspect, the present invention provides a transgenic plant that has integrated into its genome an exogenous polynucleotide encoding a polypeptide that confers resistance to at least one strain of Puccinia graminis, wherein the polypeptide comprises amino acids having a sequence as provided in SEQ ID NO: 1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO: 1, and wherein the polynucleotide is operatively linked to a promoter capable of directing the expression of the polynucleotide in a plant cell. In one embodiment, Puccinia graminis is Puccinia graminis f. sp. tritici. In one embodiment, Puccinia graminis f. sp. tritici is a breed of Ug99 or DIGALU. In one embodiment, the strain is one or more or all of the race TTRTF, PTKST, TKKTF, TKTTF and PCHSF of Puccinia graminis f. sp. tritici. In one modality, the transgenic plant has improved resistance to at least one strain of Puccinia graminis compared to an isogenic plant lacking the exogenous polynucleotide. In one embodiment, the polypeptide is an Sr26 polypeptide. In one embodiment, the polynucleotide comprises nucleotides having a sequence as provided in SEQ ID NO:2, a sequence that is at least 70% identical to SEQ ID NO:2, or a sequence that hybridizes with SEQ ID NO:2. In a further embodiment, (i) the polypeptide comprises amino acids having a sequence that is at least 90% identical to SEQ ID NO:1, and / or (ii) the polynucleotide comprises a sequence that is at least 90% identical to SEQ ID NO: 2. In one embodiment, the polypeptide comprises one or more, preferably all, of a coiled domain (CC), a nucleotide-binding domain (NB), and a leucine-rich repeat (LRR) domain. In a further embodiment, the polypeptide comprises one or more, preferably all, of a p-loop motif, a kinase 2 motif, and a kinase 3a motif in the NB domain. In one embodiment, the loop motif p comprises the sequence GxxGxGK(T / S)T (SEQ ID NO:20), more preferably the sequence GSGGMGKTT (SEQ ID NO:21). In one embodiment, the loop motif p comprises the sequence VSIVGSGGMGKTTL (SEQ ID NO:22). In one embodiment, the kinase 2 motif comprises the sequence DDxW (SEQ ID NO:23), more preferably the sequence DDIW (SEQ ID NO:24). In one embodiment, the kinase 2 motif comprises the sequence RYFWLDDIWDW (SEQ ID NO:25). In one embodiment, the kinase 3a motif comprises the sequence GxxxxxTxR (SEQ ID NO:26), more preferably the sequence GSIIITTTR (SEQ ID NO:27). In one embodiment, the kinase 3a motif comprises the sequence GSIIITTTRINEV (SEQ ID NO:28). In an additional modality, the LRR domain comprises approximately 5 to approximately 15 imperfect repetitions of the sequence xxLxLxxxx (SEQ ID NO:29). Preferably, the plant is a cereal plant. Examples of transgenic cereal plants of the invention include, but are not limited to, wheat, barley, maize, rice, oats, and triticale. In a particularly preferred embodiment, the plant is wheat. In one further embodiment, the plant comprises one or more additional exogenous polynucleotides encoding another plant pathogen resistance polypeptide. Examples of such other plant pathogen resistance polypeptides include, but are not limited to, Lr34, Lr1, Lr3, Lr2a, Lr3ka, Lr11, Lr13, Lr16, Lr17, Lr18, Lr21, LrB, Lr67, Lr46, Sr50, Sr33, Sr13, and Sr35. In one embodiment, the plant further comprises Lr34, Lr67, and Lr46. Preferably, the plant is homozygous for the exogenous polynucleotide. In one modality, the plant grows in a field. A population of at least 100 transgenic plants of the invention growing in a field is also provided. In another aspect, the present invention provides a process for identifying a polynucleotide encoding a polypeptide that confers resistance to at least one strain of Puccinia graminis, comprising: (i) obtaining a polynucleotide operationally linked to a promoter, wherein the polynucleotide encodes a polypeptide comprising amino acids having a sequence as provided in SEQ ID NO:1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO:1, QRbQQn / iznz / q / YILI i) introduce the polynucleotide into a plant, i) determine whether the level of resistance to Puccinia graminis is modified in relation to an isogenic plant lacking the polynucleotide, and iv) optionally, select a polynucleotide that when expressed confers resistance to Puccinia graminis. In one embodiment, the polynucleotide comprises nucleotides having a sequence as provided in SEQ ID NO:2, a sequence that is at least 82% identical to SEQ ID NO:2, or a sequence that hybridizes with SEQ ID NO:2. In another sense, the plant is a cereal plant such as a wheat, barley, or triticale plant. In another form, the polypeptide is a plant polypeptide or a mutant of it. In another modality, step i) also includes stably integrating the operationally linked polynucleotide into a promoter in the plant genome. In one embodiment, the strain is one or more or all of the race TTRTF, PTKST, TKKTF, TKTTF and PCHSF of Puccinia graminis f. sp. tritici. Also provided is a substantially purified and / or recombinant polypeptide conferring resistance to at least one strain of Puccinia graminis, wherein the polypeptide comprises amino acids having a sequence as provided in SEQ ID NO: 1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO: 1. In one embodiment, the polypeptide is an Sr26 polypeptide. In one embodiment, the polypeptide comprises amino acids having a sequence that is at least 80% identical, at least 90% identical, or at least 95% identical to SEQ ID NO: 1. In one embodiment, a polypeptide of the invention is a fusion protein further comprising at least one other polypeptide sequence. The at least one other polypeptide may be, for example, a polypeptide that enhances the stability of a polypeptide of the present invention, or a polypeptide that aids in the purification or detection of the fusion protein. In a further aspect, the present invention provides an isolated and / or exogenous polynucleotide comprising nucleotides having a sequence as provided in SEQ ID NO: 2, a sequence that is at least 70% identical to SEQ ID NO: 2, a sequence encoding a polypeptide of the invention, or a sequence that hybridizes with SEQ ID NO: 2. In another aspect, the present invention provides a chimeric vector comprising the polynucleotide of the invention. Preferably, the polynucleotide is operatively linked to a promoter. QAfrQQn / L7n7 / 3 / YILI In a further aspect, the present invention provides a recombinant cell comprising an exogenous polynucleotide of the invention and / or a vector of the invention. The cell can be any type of cell such as, among others, a plant cell, a bacterial cell, an animal cell, or a yeast cell. Preferably, the cell is a plant cell. Preferably, the plant is a cereal plant. Even more preferably, the cereal plant cell is a wheat cell. In a further aspect, the present invention provides a method for producing the polypeptide of the invention, wherein the method comprises expressing the polynucleotide of the invention in a cell or cell-free expression system. Preferably, the method also includes isolating the polypeptide. In another aspect, the present invention provides a transgenic non-human organism comprising an exogenous polynucleotide of the invention, a vector of the invention and / or a recombinant cell of the invention. Preferably, the transgenic non-human organism is a plant. Preferably, the plant is a cereal plant. Preferably, the cereal plant is a wheat plant. In another aspect, the present invention provides a method for producing the cell of the invention, wherein the method comprises the step of introducing the polynucleotide of the invention, or a vector of the invention, into a cell. Preferably, the cell is a plant cell. In a further aspect, the present invention provides a method for producing a transgenic plant of the invention, wherein the method comprises the steps of i) introducing a polynucleotide of the invention and / or a vector of the invention into a plant cell, ii) regenerating a transgenic plant from the cell, and iii) optionally harvesting seeds from the plant, and / or iv) optionally producing one or more offspring plants from the transgenic plant, thereby producing the transgenic plant. In a further aspect, the present invention provides a method for producing a transgenic plant of the invention, wherein the method comprises the steps of i) crossing two parent plants, wherein at least one plant is a transgenic plant of the invention, ii) screening one or more offspring plants from the cross to detect the presence or absence of the polynucleotide, and iii) selecting an offspring plant comprising the polynucleotide, QAfrQQn / 1 znz / q / ΥΙΛΙ thus producing the plant. In one embodiment, at least one of the parent plants is a transgenic plant of the invention, and the selected offspring plant comprises an exogenous polynucleotide encoding a polypeptide that confers resistance to at least one strain of Puccinia graminis. In an additional modality, at least one of the parent plants is a tetraploid or hexeploid wheat plant. In other modelided further, le etepe ¡i) comprises enelizer une muestra que compren ADN de le píente pere el polinucleotide. In another model, the step iii) comprises i) select descendants plants that are homozygous for the polynucleotide, and / or i) select the plant or one or more descendants plants of the same to determine the resistance of the least one strain of Puccinia graminis. In one model, the cepe is one or more or all of the reze TTRTF, PTKST, TKKTF, TKTTF and PCHSF of Puccinia graminis f. sp. tritici. In a modeled way, the method also comprises iii) backcrossing the offspring of the cross of step i) with plants of the same genotype as a first parent plant that possesses a polynucleotide that encodes a polypeptide that confers resistance to at least one strain of Puccinia graminis a sufficient number of times to produce a plant with the majority of the genotype of the first parent but that comprises the polynucleotide, and iv) selecting a descendant plant that has resistance to at least one strain of Puccinia graminis. In another space, a method of the invention comprises also the step of enelizer the píente in busce of the least other genetic merchant. A ping produced using a method of the invention is also provided. The use of the polynucleotide of the invention, or a vector of the invention, to produce a recombinant cell and / or a transgenic plant is also provided. In one model, the transgenic plant has improved resistance to at least one strain of Puccinia graminis compared to an isogenic plant lacking the exogenous polynucleotide and / or vector. In an editorial space, the present invention provides a method to identify a ping comprising a polynucleotide encoding a polypeptide that confers resistance to at least one strain of Puccinia graminis, where the method comprises the steps of i) obtain a nucleic acid sample from a plant, and ii) screen the sample to detect the presence or absence of the polynucleotide, wherein the polynucleotide encodes a polypeptide of the invention. QAfrQQn / 1 znz / q / YILI In one embodiment, the polynucleotide comprises nucleotides having a sequence as provided in SEQ ID NO:2, a sequence that is at least 70% identical to SEQ ID NO:2, or a sequence that hybridizes with SEQ ID NO:2. In one embodiment, the method identifies a transgenic plant of the invention. In another modality, the method also includes producing a plant from a seed before stage i). A plant layout of the invention is also provided. In one embodiment, the plant part is a seed comprising an exogenous polynucleotide encoding a polypeptide that confers resistance to at least one strain of Puccinia graminis. In a further aspect, the present invention provides a method for producing a plant part, wherein the method comprises, a) cultivate a plant of the invention, and b) harvest the plant part. In another aspect, the present invention provides a method for producing flour, wholemeal flour, starch, or other product obtained from seeds, wherein the method comprises; a) obtain the seed of the invention, and b) extract the flour, wholemeal flour, starch or other product. In an additional aspect, the present invention provides a product produced from a plant of the invention and / or a part of a plant of the invention. In one modality, the part is a seed. In one modality, the product is a food product or a beverage product. Examples include, but are not limited to; i) the selected food product from the group consisting of: flour, starch, leavened or unleavened breads, pasta, noodles, animal fodder, animal feed, breakfast cereals, snacks, cakes, malt, beer, pastries and foods containing flour-based sauces, or i) the drinkable product which is beer or malt. In an alternative scenario, the product is a non-food item. Examples include, but are not limited to, films, coatings, adhesives, building materials, and packaging materials. In a further aspect, the present invention provides a method for preparing a food product of the invention, wherein the method comprises mixing seeds, or flour, wholemeal flour or seed starch, with another food ingredient. QAfrQQn / L7n7 / 3 / YILI In another aspect, the present Invention provides a method for preparing malt, comprising the stage of germinating the seed of the invention. The use of a plant of the invention, or part thereof, as animal feed, or to produce food for animal consumption or food for human consumption is also provided. In a further aspect, the present invention provides a composition comprising one or more of a polypeptide of the invention, a polynucleotide of the invention, a vector of the invention, or a recombinant cell of the invention and one or more acceptable carriers. In another aspect, the present invention provides a method for identifying a compound that binds to a polypeptide comprising amino acids having a sequence as provided in SEQ ID NO: 1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO: 1, wherein the method comprises: i) contacting the polypeptide with a candidate compound, and i) determining whether the compound binds to the polypeptide. Any modality hereof shall be deemed to apply mutatis mutandis to any other modality unless specifically stated otherwise. The scope of the present invention shall not be limited to the specific embodiments described herein, which are provided for illustrative purposes only. Functionally equivalent products, compositions, and methods are clearly within the scope of the invention as described herein. Throughout this descriptive report, unless specifically stated otherwise or the context requires otherwise, reference to a single stage, material composition, group of stages, or group of material compositions should be considered to encompass both one and a plurality (i.e., one or more) of such stages, material compositions, groups of stages, or groups of material compositions. The invention is described below by means of the following non-limiting examples and with reference to the accompanying figures. BRIEF DESCRIPTION OF THE ATTACHED FIGURES Figure 1 - Phenotypic responses to Puccinia graminis of the wild-type and Sr26 mutant 12S line and schematic gene structure of Sr26. a. Susceptible mutant Sr26 line derived from Avocet EMS and wild-type Avocet (12S1 with an S431N mutation) inoculated with PTKST isolated from Pgt of the Ug99 lineage at the seedling and adult plant stages, b. Structures QAfrQQn / L7n7 / 3 / YILI of candidate genes (top), with mutations and their predicted effects on the identified translated protein. The predicted conserved domains for the CNL protein are shown corresponding to the gene structure (bottom). Figure 2 - Wild-type and EMS-derived mutants used in the MuRenSeq ensemble. a. Five mutants and wild-type mutants used for the MuRenSeq ensemble to identify the candidate gene Sr26; b. IGV snapshot showing the SNP changes in each mutant line used. The screenshot illustrates the Sr26 locus with four identified susceptible mutants, all carrying a mutation in the candidate contig, and one deletion mutant that has no read mapping in the wild-type assembly. The entire locus was assembled de novo. From top to bottom: horizontal lines represent the orientation of the identified contig, while read coverage (gray histograms) is indicated on the left, e.g., [0–1651], and the name of the line from which the reads are derived is shown on the right. Vertical bars represent the position of the identified SNPs between the reads and the reference assembly.The rectangles represent the motifs identified by NLR-Parser (each motif is specific to a conserved NLR domain). Note that the orientation of this IGV snapshot is 3' to 5'; therefore, all SNPs are actually a G-to-A mutation. The 12S and 70S mutants are likely siblings due to their possession of identical SNPs. Figure 3 - The CC (coil), NB-ARC (nucleotide-binding), and LRR (leucine-rich repeat) domains are indicated by bars. Conserved motifs (EDVID, kinase 2, RNBS-B, kinase 3 (RNBS-C), GLPL, RNBS-D, and MHDV) are indicated by frames and labeled below the sequence. The sequence marked with stars shows the position of amino acid changes that led to the loss of functional mutations. Sr26wtNLR682 and Sr26wtNLR682 are two NLR contigs that have the greatest similarity to the Sr26 candidate gene from wild-type de novo assembly. Alignment with other Sr protein sequences, Sr13, Sr21, Sr22, Sr33, Sr25, Sr45, and Sr50, is shown. Figure 4 - Transgenic validation of Sr26. Three constructs in the T0 generation inoculated by Pgt 98-1,2,3,5,6. a. Three constructs were used for the validation of the transformation of the candidate gene Sr26. b. Representative phenotypic response to Pgt of T0 plants of each construct. QAfrQQn / L7n7 / 3 / YILI Figure 5 - Location of the closest homologs of the Sr26 gene sequence in grass and diploid wheat genomes. Figure 6 - Phylogenetic analysis of R genes. Figure 7 - Induction of cell death by the CC domains of the wheat Sr gene in plants. (A) Partial alignment of the sequences of the proteins Sr33, Sr50, Sr26, Sr22, Sr35, Sr45, and Sr46 showing the site corresponding to residue 160 of Sr33. (B) Protein fragments Sr331-160, Sr501-163, Sr261-163, Sr221-168, Sr351-161, Sr451-163, and Sr461-171 fused at the N-terminus to YFP were transiently expressed in N. benthamiana. The self-active Sr50CCYFP and YFP were used as positive and negative controls, respectively. Cell death was documented 5 days after infiltration. Equivalent results were obtained in three independent experiments. (C) The indicated proteins, transiently expressed in N. benthamiana leaves, were extracted 24 hours after infiltration and analyzed by immunoblotting with anti-GFP antibodies (α-GFP).Ponceau staining of the large subunit of RubisCO (ribulose-1,5-bisphosphate carboxylase / oxygenase) shows the same protein loading. Figure 8 - Untagged Sr22 and Sr45 protein fragments were transiently expressed in N. benthamiana. The self-active Sr50CC-YFP and YFP were used as positive and negative controls, respectively. Cell death was documented 5 days after infiltration. Equivalent results were obtained in three independent experiments. Figure 9 - Synergistic resistance to stem rust observed in wheat seedlings and adult plants inoculated with the Pgt PTKST pathotype of the Ug99 lineage. Line labeling order: 1. Kite; 2. Avocet+L / ^S; 3. kvocet+Lr34+Lr46+Lr67; 4. Line 37-07 (control); 5. Sr26 12S mutant; 6. Sr26 499S mutant. a. Stem rust response observed at 12 dpi in the seedling stage under greenhouse conditions; b. Stem rust response observed at 14 dpi in flag leaves of adult plants under greenhouse conditions; c. First round of stem rust response observed in stems of adult plants under field conditions; d. Second round of stem rust response observed in stems of adult plants under field conditions (21 days after the first round); e. Representative colony size differences observed in the flag leaf sheath of the adult plant at 4 dpi under greenhouse conditions; g.Panoramic comparison of colony size between Avocet+ Lr34+Lr46+Lr67 (No. 3) and Sr26 mutant 12S (No. 5). QRbQQn / \7(\7Ί / YΙΛΙ Figure 10 - Stem rust responses of flag leaves and stems when inoculated with the Pgt PTKST pathotype of the Ug99 lineage at the adult plant stage. Line labeling order: 1. Kite; 2. Avocet+L / ^G; 3. Avocet+Lr34+Lr46+Lr67; 4. Line 37-07 (control); 5. Sr26 mutant 12S; 6. Sr26 mutant 499S. a. Stem rust response observed at 20 dpi in flag leaves of adult plants under greenhouse conditions; b. Stem rust response observed at 20 dpi in stems of adults under greenhouse conditions; c. Chitin assay results from the flag leaf sheath at 14 dpi at the adult plant stage; d. Measurements of the average size of individual colonies on the flag leaf sheath of adult plants at 4 dpi under greenhouse conditions. All results were obtained based on three biological and technical replicates. KEY FOR SEQUENCE LISTING SEQ ID NO:1 - Amino acid sequence of the stem rust-resistant polypeptide Sr26. SEQ ID NO:2 - Open reading frame encoding the polypeptide Sr26. SEQ ID NO:3 - Amino acid sequence of the polypeptide Sr13 (ATE88995.1). SEQ ID NO:4 - Amino acid sequence of the polypeptide Sr21 (AVK42833.1). SEQ ID NO:5 - Amino acid sequence of the polypeptide Sr22 (CUM44200.1). SEQ ID NO:6 - Amino acid sequence of the polypeptide Sr33 (AGQ17386.1). SEQ ID NO:7 - Amino acid sequence of the polypeptide Sr35 (AGP75918.1). SEQ ID NO:8 - Amino acid sequence of the polypeptide Sr45 (CUM44213.1). SEQ ID NO:9 - Amino acid sequence of the Sr50 polypeptide (ALO61074.1). SEQ ID NO: 10 - Amino acid sequence of the Chinese Spring6A protein. SEQ ID NO:11 - Amino acid sequence of the Chinese Spring6B protein. SEQ ID NO:12 - Amino acid sequence of the Chinese Spring6C protein. SEQ ID NO: 13 - Genomic sequence that encodes the Sr26 polypeptide. SEQ ID NO:14 - Fragment of Sr33. SEQ ID NO:15 - Fragment of Sr50. SEQ ID NO: 16 - Fragment of Sr26. SEQ ID NO: 17 - Fragment of Sr22. SEQ ID NO: 18 - Fragment of Sr45. SEQ ID NO: 19 - Fragment of Sr46. SEQ ID NQ:20 - loop consensus motif p. SEQ ID NO:21 - Sr26 loop motif p. SEQ ID NO:22 - Sr26 extended loop reason p. QAfrQQn / 1 znz / q / YILI SEQ ID NO:23 - reason for consensus kinase 2. SEQ ID NO:24 - Sr26 kinase motif 2. SEQ ID NO:25 - Sr26 extended kinase 2 motif. SEQ ID NO:26 - reason for consensus kinase 3a. SEQ ID NO:27 - Sr26 kinase 3a motif. SEQ ID NO:28 - Sr26 extended kinase 3a motif. SEQ ID NO:29 - LRR domain repetition consensus sequence. SEQ ID NO 30 and 31: oligonucleotide primers. DETAILED DESCRIPTION OF THE INVENTION General definitions and techniques Unless specifically defined otherwise, all technical and scientific terms used herein shall be deemed to have the same meaning as commonly understood by a person skilled in the art (e.g., in cell culture, molecular genetics, plant molecular biology, protein chemistry, and biochemistry). Unless otherwise stated, the recombinant protein, cell culture, and immunological techniques used in the present invention are standard procedures, well known to those skilled in the art. Such techniques are described and explained throughout the literature in sources such as J. Perbal, A Practical Guide to Molecular Cloning, John Wiley and Sons (1984), J. Sambrook et al., Molecular Cloning: A Laboratory Manual, Coid Spring Harbour Laboratory Press (1989), T.A. Brown (editor), Essential Molecular Biology: A Practical Approach, Volumes 1 and 2, IRL Press (1991), D.M. Glover and B.D. Hames (editors), DNA Cloning: A Practical Approach, Volumes 1-4, IRL Press (1995 and 1996), and F.M. Ausubel et al. (editors), Current Protocols in Molecular Biology, Greene Pub. Associates and Wiley-Interscience (1988, including all patents to date), Ed Harlow and David Lane (editors) Antibodies: A Laboratory Manual, Cold Spring Harbour Laboratory, (1988), and JEColigan et al. (editors) Current Protocols in Immunology, John Wiley & Sons (including all updates to date). The term “and / or”, e.g., “X and / or Y” shall be understood to mean either “X and Y” or “X or Y” and shall be deemed to provide explicit support for either or both meanings. Throughout this descriptive report, the word includes, or variations such as comprising or comprising, shall be understood to imply the inclusion of an element, whole number or stage, or group of elements, whole numbers or stages established, but not the exclusion of any other element, whole number or stage, or group of elements, whole numbers or stages. QAfrQQn / L7n7 / 3 / YILI Polypeptides As used herein, the term Sr26 refers to a family of proteins that share a high primary amino acid sequence identity, for example, at least 70%, at least 80%, at least 90%, or at least 95% identity with the amino acid sequences provided as SEQ ID NO:1. The inventors hereof have determined that some variants of the Sr26 protein family, when expressed in a plant, confer resistance to at least one strain of Puccinia graminis. An example of such a variant comprises an amino acid sequence provided as SEQ ID NO:1. Accordingly, variants that confer resistance are herein referred to as Sr26 (resistant) polypeptides or proteins, while those that do not (see the mutants mentioned in Figure 2a) are herein referred to as Sr26 (susceptible) polypeptides.In a preferred embodiment, the Sr26 (resistant) proteins do not comprise a mutation, such as a threonine, at a position corresponding to amino acid number 311 of SEQ ID NO:1, or a mutation, such as an asparagine, at a position corresponding to amino acid number 431 of SEQ ID NO:1, or a deletion in the RNBS-D motif, such as one or more or all of the amino acids at a position corresponding to amino acid numbers 447 to 468 of SEQ ID NO:1. The polypeptides of the invention typically comprise a coiled domain (CC) toward the N-terminus, followed by a nucleotide-binding domain (NB) and a leucine-rich repeat (LRR) domain toward the C-terminus (see Figure 1b). Each of these three domain types is common in polypeptides that confer resistance to plant pathogens. Furthermore, CC-NB-LRR-containing polypeptides are a well-known class of polypeptides that, as a class, confer resistance to a wide variety of different plant pathogens (see, for example, Bulgarelli et al., 2010; McHale et al., 2006; Takken et al., 2006; Wang et al., 2011; Gennaro et al., 2009; and Dilbirligi et al., 2003), although each CC-NB-LRR polypeptide is specific to a particular species or subspecies of pathogen.Therefore, by aligning the polypeptides of the invention with other CC-NB-LRR polypeptides, combined with the large number of studies on these types of proteins, as well as CC domains, NB domains, and LRR domains, the person skilled in the art has a considerable amount of guidance for designing functional variants of the specific polypeptides provided herein (as provided in Figure 3). A coiled domain or motif is a structural motif that is one of the most common tertiary structures of proteins, where helices coil together like strands of a rope. Computer programs have been designed to detect heptas and yield coiled coil structures (see, for example, Delorenzi and Speed, 2002). Coiled coils typically comprise a repeating pattern, hxxhcxc, of residues of QAfrQQn / L7n7 / 3 / YILI hydrophobic (h) and charged (c) amino acids, called heptad repeats. The positions in the heptad repeat are usually labeled abcdefg, where a and d are the hydrophobic positions, often occupied by isoleucine, alanine, leucine, or valine. Folding a protein with these hepatates into a helical secondary structure causes the hydrophobic residues to appear as a strip that gently wraps around the left-handed helix, forming an amphipathic structure. The NB domain is present in resistance genes, as well as in several kinases such as ATP / GTP-binding proteins. This domain typically contains three motifs: kinase-1a (p-loop), a kinase-2, and a putative kinase-3a (Traut 1994; Tameling et al., 2002). The consensus sequence of GxxGxGK(T / S)T (SEQ ID NO:20) (GSGGMGKTT (SEQ ID NO:21) in the polypeptide conferring resistance to Puccinia graminis provided as SEQ ID NO:1), DDxW (SEQ ID NO:23) (DDVW (SEQ ID NO:24) in the polypeptide conferring resistance to Puccinia graminis provided as SEQ ID NO:1) and GxxxxxTxR (SEQ ID NO:26) (GSIIITTTR (SEQ ID NO:27) in the polypeptide conferring resistance to Puccinia graminis provided as SEQ ID NO:1) for the p-loop resistance gene motifs, kinase-2 and putative kinase-3a, respectively, are different from those present in other NB-encoding proteins.Other motifs present in the NB domain of NB / LRR-type resistance genes are GLPL, RNBS-D, and MHD (Meyers et al., 1999). The sequences interspersed among these motifs and domains can be very different even between homologs of a resistance gene (Michelmore and Meyers, 1998; Pan et al., 2000). A leucine-rich domain (LRR) is a protein structural motif that forms an α / β horseshoe fold (Enkhbayar et al., 2004). The LRR domain contains 9–41 imperfect repeats, each approximately 25 amino acids in length with a consensus amino acid sequence of xxLxLxxxx (SEQ ID NO: 29) (Cooley et al., 2000). In one embodiment, a polypeptide of the invention comprises approximately 5 to approximately 15, more preferably approximately 10 to approximately 14, and more preferably approximately 12 leucine-rich repeats. These repeats commonly fold together to form a solenoid protein domain. Typically, each repeat unit has an alpha-turn-beta-strand structure, and the assembled domain, composed of many of these repeats, is horseshoe-shaped with an inner parallel beta-sheet and an outer array of helices. As used herein, resistance is a relative term in the sense that the presence of a polypeptide of the invention (i) reduces the disease symptoms of a plant comprising the gene (R (resistant) gene) conferring resistance, relative to a plant lacking the R gene, and / or (ii) reduces the reproduction or spread of pathogens in a plant or within a population of plants comprising the R gene. Resistance, as used herein The presence of the R gene in this invention relates to the susceptible response of a plant to the same pathogen. Typically, the presence of the R gene enhances at least one production trait of a plant containing the R gene when infected with the pathogen, such as grain yield, compared to an isogenic plant infected with the pathogen but lacking the R gene. The isogenic plant may have some level of resistance to the pathogen or may be classified as susceptible. Therefore, the terms resistance and enhanced resistance are generally used interchangeably herein. Furthermore, a polypeptide of the invention does not necessarily confer complete resistance to pathogens, for example, when some symptoms still occur or there is some pathogen reproduction in the infection, but in a reduced amount within a plant or plant population.Resistance may occur only at certain stages of plant growth, for example, in adult plants (fully grown) and less so, or not at all, in seedlings, or at all stages of plant growth. In one embodiment, resistance occurs at both the adult and seedling stages. By using a transgenic strategy to express an Sr26 polypeptide in a plant, resistance can be provided to the plant of the invention throughout its growth and development. The enhanced resistance can be determined by various methods known in the art, such as analyzing plants to determine the amount of pathogen and / or analyzing plant growth or the amount of damage or disease symptoms in a plant in the presence of the pathogen, and comparing one or more of these parameters with an isogenic plant lacking an exogenous gene encoding a polypeptide of the invention. A substantially purified polypeptide or purified polypeptide means a polypeptide that has generally been separated from the lipids, nucleic acids, other peptides, and other contaminating molecules with which it is associated in its native state. Preferably, the substantially purified polypeptide is at least 90% free of other components with which it is naturally associated. In one embodiment, the polypeptide of the invention has an amino acid sequence that differs from a naturally occurring Sr26 polypeptide; that is, it is an amino acid sequence variant. The transgenic plants and host cells of the invention may comprise an exogenous polynucleotide encoding a polypeptide of the invention. In these cases, the plants and cells produce a recombinant polypeptide. The term recombinant in the context of a polypeptide refers to the polypeptide encoded by an exogenous polynucleotide when produced by a cell, a polynucleotide that has been introduced into the cell or a precursor cell by recombinant DNA or RNA techniques such as, for example, transformation. Typically, the cell comprises a non-endogenous gene that causes the production of an altered amount of the polypeptide. In one embodiment, a polypeptide QAfrQQn / 1 znz / q / YILI recombinant is a polypeptide made by expressing an exogenous (recombinant) polynucleotide in a plant cell. The terms polypeptide and protein are generally used interchangeably. The percent identity of a polypeptide is determined by GAP analysis (Needleman and Wunsch, 1970) (GCG program) with a gap creation penalty of 5 and a gap extension penalty of 0.3. The query sequence is at least 500 amino acids long, and the GAP analysis aligns the two sequences in a region of at least 500 amino acids. More preferably, the query sequence is at least 750 amino acids long, and the GAP analysis aligns the two sequences in a region of at least 750 amino acids. Even more preferably, the query sequence is at least 900 amino acids long, and the GAP analysis aligns the two sequences in a region of at least 900 amino acids. Even more preferably, the GAP analysis aligns two sequences along their entire length, which for a polypeptide Sr26 is approximately 935 amino acid residues. As used herein, a biologically active fragment is a portion of a polypeptide of the invention that maintains a defined activity of the full-length polypeptide, such that when expressed in a plant, such as wheat, it confers (enhanced) resistance to stem rust caused by at least one strain of Puccinia graminis compared to an isogenic plant that does not express the polypeptide. Biologically active fragments may be of any size, provided they maintain the defined activity, but preferably are at least 750 or at least 900 amino acid residues in length. Preferably, the biologically active fragment maintains at least 10%, at least 50%, at least 75%, or at least 90% of the activity of the full-length protein. In one embodiment, the biologically active fragment comprises CC, NB, and LRR functional domains. With respect to a defined polypeptide, it will be appreciated that higher % identity figures than those provided above will encompass preferred embodiments. Therefore, where appropriate, in light of the minimum % identity figures, it is preferred that the polypeptide comprise an amino acid sequence that is preferably at least 70%, more preferably at least 75%, more preferably at least 76%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 91%, more preferably at least 92%, more preferably at least 93%, more preferably at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, more preferably at least 99%, more preferably at least 99.1%, more preferably at least 99.2%, more preferably at least 99.3%, and more preferably at least 99.4%, more preferably at least 99.5%, more preferably at least 99.6%, more. QAfrQQn / Lznz / q / YILI preferably at least 99.7%, more preferably at least 99.8%, and even more preferably at least 99.9% identical to the relevant SEQ ID NO. named. In one embodiment, a polypeptide of the invention is not a naturally occurring polypeptide. As used herein, the phrase "in a position corresponding to the number of amino acids or variations thereof" refers to the relative position of the amino acid compared to the surrounding amino acids. In this respect, in some embodiments, a polypeptide of the invention may have a deletion or substitution mutation that alters the relative positioning of the amino acid when aligned against, for example, SEQ ID NO:1. Amino acid sequence mutants of the polypeptides of the present invention can be prepared by introducing appropriate nucleotide changes into a nucleic acid of the present invention, or by in vitro synthesis of the desired polypeptide. Such mutants include, for example, deletions, insertions, or substitutions of residues within the amino acid sequence. A combination of deletion, insertion, and substitution can be performed to arrive at the final construct, provided that the final peptide product possesses the desired characteristics. The preferred amino acid sequence mutants have only one, two, three, four, or fewer than 10 amino acid changes with respect to the reference wild-type polypeptide. Mutant (altered) polypeptides can be prepared using any known technique, for example, using directed evolution or rational design strategies (see below). Products derived from mutated / altered DNA can be readily screened using techniques described herein to determine whether, when expressed in a plant such as wheat, they confer (enhanced) resistance to at least one strain of Puccinia graminis. For example, the method may involve producing a transgenic plant expressing the mutated / altered DNA and determining the effect of the pathogen on plant growth. When designing amino acid sequence mutants, the location of the mutation site and the nature of the mutation will depend on the characteristic or characteristics to be modified. Mutation sites can be modified individually or serially, for example, (1) by first substituting them with conservative amino acid choices and then with more radical selections depending on the results obtained, (2) by deleting the target residue, or (3) by inserting other residues adjacent to the localized site. Deletions of the amino acid sequence generally range from approximately 1 to 15 residues, more preferably from approximately 1 to 10 residues and typically from approximately 1 to 5 contiguous residues. Substitution mutants have at least one amino acid residue in the polypeptide molecule removed and a different residue inserted in its place. When maintaining a certain level of activity is desirable, it is preferable to avoid substitutions, or to perform only substitutions. Conservative substitutions are found at amino acid positions that are highly conserved in the relevant protein family. Table 1 shows examples of conservative substitutions under the heading of exemplary substitutions. In a preferred embodiment, the mutant / variant polypeptide has one, two, three, or four conservative amino acid changes compared to a naturally occurring polypeptide. Details of the conservative amino acid changes are provided in Table 1. In a preferred embodiment, the changes are not in one or more of the motifs that are highly conserved among the different polypeptides provided herein and / or are not in the major motifs of Sr26 polypeptides identified herein. As those skilled in the art will know, it can be reasonably predicted that such minor changes will not alter the activity of the polypeptide when expressed in a recombinant cell. The primary amino acid sequence of a polypeptide of the invention can be used to design variants / mutants thereof based on comparisons with closely related polypeptides (e.g., as shown in Figure 3). As the knowledgeable recipient will appreciate, highly conserved residues among closely related proteins are less likely to be altered, especially with non-conservative substitutions, and to maintain activity than less conserved residues (see above). Table 1. Exemplary substitutions. QAfrQQn / 1 znz / q / YILI Original Residue Exemplary Substitutions Ala (A) val; leu; you; gly Arg (R) lys Asn (N) gln; his Asp (D) glu Cys (C) ser Gln (Q) asn; his Glu (E) asp Gly (G) pro, ala His (H) asn; gln lle(l) leu; val; ala Leu (L) ¡le; val; met; to the; phe Lys (K) arg Met (M) leu; phe Phe(F) leu; val; ala Pro (P) giy Ser(S) thr Thr(T) ser Trp (W) tyr Tyr (Y) trp; phe Val (V) ¡le; leu; met; phe, wing QAfrQQn / L7n7 / 3 / YILI Also included within the scope of the invention are polypeptides of the present invention that are differentially modified during or after synthesis, for example, by biotinylation, benzylation, glycosylation, acetylation, phosphorylation, amidation, derivatization by protecting / blocking groups, proteolytic cleavage, attachment to an antibody molecule or other cellular ligand, etc. The polypeptides can be post-translationally modified in a cell, for example, by phosphorylation, which can modulate their activity. These modifications can serve to increase the stability and / or bioactivity of the polypeptide of the invention. Directed evolution In directed evolution, random mutagenesis is applied to a protein, and a selection regime is used to select for variants with desired qualities, such as increased activity. Further rounds of mutation and selection are then applied. A typical directed evolution strategy involves three stages: 1) Diversification: the gene that codes for the protein of interest is randomly mutated and / or recombined to create a large library of gene variants. Variant gene libraries can be constructed by error-prone PCR (see, for example, Leung, 1989; Cadwell and Joyce, 1992), from groups of DNA-digested fragments prepared from parental templates (Stemmer, 1994a; Stemmer, 1994b; Crameri et al., 1998; Coco et al., 2001), from degenerate oligonucleotides (Ness et al., 2002, Coco, 2002), or from mixtures of both, or even from undigested parental templates (Zheo et al., 1998; Eggert et al., 2005; Jézéquek et al., 2008), and generally assembled by PCR. Libraries can also be prepared from parent sequences recombined in vivo or in vitro by homologous or non-homologous recombination (Ostermeier et al., 1999; Volkov et al., 1999; Sieber et al., 2001).Variant gene libraries can also be constructed by subcloning a gene of interest into a suitable vector, transforming the vector into a mutator strain such as E. coli XL-'i red (Stratagene), and propagating the transformed bacteria for a suitable number of generations. Variant gene libraries can also be constructed by subjecting the gene of interest to a mixture of DNA (i.e., in vitro homologous recombination of selected mutant gene clusters by random fragmentation and reassembly), as extensively described by Harayama (1998). 2) Screening: The library is tested for the presence of mutants (vanants) possessing the desired property using a screening or selection process. Screenings allow for the manual identification and isolation of high-throughput mutants, while selections automatically eliminate all non-functional mutants. A screening process may involve testing for the presence of known conserved amino acid motifs. Alternatively, or in addition, a screening process may involve expressing the mutated polynucleotide in a host organism or part thereof and testing the level of activity. 3) Amplification: the variants identified in the selection or screening are replicated many times, allowing researchers to sequence their DNA to understand what mutations have occurred. Together, these three stages are called a directed evolution round. Most experiments will involve more than one round. In these experiments, the winners from the previous round are diversified in the next round to create a new library. At the end of the experiment, all evolved mutant proteins or polynucleotides are characterized using biochemical methods. Rational design A protein can be rationally designed based on known information about its structure and folding. This can be achieved through design from scratch (de novo design) or through redesign based on native scaffolds (see, for example, Hellinga, 1997; and Lu and Berry, Protein Structure Design and Engineering, Handbook of Proteins 2, 1153–1157 (2007)). Protein design typically involves identifying sequences that fold into a given or target structure and can be accomplished using computer models. Computational protein design algorithms search the conformation space of sequences for low-energy sequences when folded into the target structure. These algorithms use protein energy models to assess how mutations would affect a protein's structure and function.These energy functions typically include a combination of molecular mechanics, statistics (i.e., knowledge-based), and other empirical terms. Suitable software is available. QAfrQQn / L7n7 / 3 / YILI IPRO (intensive protein redesign and optimization), EGAD (a genetic algorithm for protein design), Rosetta Design, Sharpen, and Abalone. Polynucleotides and genes The present invention relates to various polynucleotides. As used herein, a polynucleotide, nucleic acid, or nucleic acid molecule means a polymer of nucleotides, which may be DNA or RNA or a combination thereof, and includes genomic DNA, mRNA, cRNA, and cDNA. Less preferred polynucleotides include tRNA, siRNA, shRNA, and hpRNA. It may be DNA or RNA of cellular, genomic, or synthetic origin, for example, produced on an automated synthesizer, and may be combined with carbohydrates, lipids, proteins, or other materials, labeled with fluorescent or other groups, or attached to a solid support to perform a particular activity defined herein, or comprise one or more modified nucleotides not found in nature but well known to those skilled in the art. The polymer may be single-stranded, essentially double-stranded, or partially double-stranded.Base pairing, as used herein, refers to standard base pairing between nucleotides, including G:U base pairs. Complementary means that two polynucleotides are capable of pairing their bases (hybridizing) along part of their lengths, or along the entire length of one or both. A hybridized polynucleotide means that the polynucleotide actually has its bases paired with its complement. The term polynucleotide is used interchangeably herein with the term nucleic acid. The preferred polynucleotides of the invention encode a polypeptide of the invention. An isolated polynucleotide is a polynucleotide that has generally been separated from the polynucleotide sequences with which it is associated or linked in its native state, if the polynucleotide occurs in nature. Preferably, the isolated polynucleotide is at least 90% free of other components with which it is naturally associated, if it occurs in nature. Preferably, the polynucleotide is not of natural origin, for example, by covalently joining two shorter polynucleotide sequences in a manner not found in nature (chimeric polynucleotide). The present invention involves the modification of gene activity and the construction and use of chimeric genes. As used herein, the term gene includes any sequence of deoxyribonucleotides that includes a protein-coding region or that is transcribed in a cell but not translated, as well as associated regulatory and non-coding regions. Such associated regions are typically located adjacent to the coding or transcribed region at both the 5' and 3' ends, at a distance of approximately 2 kb on each side. In this sense, the gene may include control signals such as promoters, enhancers, and other signaling pathways. QAfrQQn / L7n7 / 3 / YILI polyadenylation and / or termination signals that are naturally associated with a given gene, or heterologous control signals, in which case the gene is called a chimeric gene. Sequences located 5' upstream of the coding region and present in mRNA are called 5' untranslated sequences. Sequences located 3' downstream of the coding region and present in mRNA are called 3' untranslated sequences. The term gene encompasses both cDNA and genomic forms of a gene. An Sr26 gene, as used herein, refers to a nucleotide sequence homologous to an isolated Sr26 cDNA (as provided in SEQ ID NO:2). As described herein, some alleles and variants of the Sr26 gene family encode a protein that confers resistance to at least one strain of Puccinia graminis. Sr26 genes include naturally occurring alleles or variants found in cereals such as wheat, as well as artificially produced variants. A genomic form or clone of a gene containing the transcribed region may be interrupted by non-coding sequences called introns, intermediate regions, or stop sequences, which may be homologous or heterologous to the gene's exons. An intron, as used herein, is a segment of a gene that is transcribed as part of a primary RNA transcript but is not present in the mature mRNA molecule. Introns are removed or spliced ​​out of the nuclear or primary transcript; therefore, introns are absent in messenger RNA (mRNA). Introns may contain regulatory elements such as enhancers. As described herein, the wheat Sr26 genes (both resistant and susceptible alleles) contain two introns in their protein-coding regions.Exons, as used herein, refers to the DNA regions corresponding to RNA sequences present in mature mRNA or in the mature RNA molecule when the RNA molecule is not translated. An mRNA functions during translation to specify the sequence or order of amino acids in a nascent polypeptide. The term gene includes a synthetic or fusion molecule encoding all or some of the proteins of the invention described herein and a nucleotide sequence complementary to any of the foregoing. A gene may be introduced into a suitable vector for extrachromosomal maintenance in a cell or, preferably, for integration into the host genome. As used herein, a chimeric gene refers to any gene comprising covalently linked sequences that are not found together in nature. Typically, a chimeric gene comprises regulatory and transcribed or protein-coding sequences that are not found together in nature. Accordingly, a chimeric gene may comprise regulatory and coding sequences that are derived from different sources, or QRbQQn / iznz / q / YILI regulatory and coding sequences derived from the same source, but arranged differently than they are found in nature. In one modality, the protein-coding region of an Sr26 gene is operatively linked to a promoter or polyadenylation / termination region that is heterologous to the Sr26 gene, thus forming a chimeric gene. The term endogenous is used herein to refer to a substance that is normally present or produced in an unmodified plant at the same stage of development as the plant under investigation. An endogenous gene refers to a gene native to its natural location in the genome of an organism. As used herein, recombinant nucleic acid molecule, recombinant polynucleotide, or variations thereof refer to a nucleic acid molecule that has been constructed or modified by recombinant DNA / RNA technology.The terms foreign polynucleotide or exogenous polynucleotide or heterologous polynucleotide and similar terms refer to any nucleic acid that is introduced into the genome of a cell through experimental manipulations. Foreign or exogenous genes can be genes inserted into a non-native organism or cell, native genes introduced into a new location within the native host, or chimeric genes. Alternatively, foreign or exogenous genes can result from editing the genome of the organism or cell, or its offspring. A transgene is a gene that has been introduced into the genome through a transformation procedure. The term genetically modified includes the introduction of genes into cells through transformation or transduction, the mutation of genes in cells, and the alteration or modulation of gene regulation in a cell or organism that has undergone these procedures, or in its offspring.Furthermore, the term exogenous in the context of a polynucleotide (nucleic acid) refers to the polynucleotide when it is present in a cell that does not naturally contain the polynucleotide. The cell may be a cell containing a non-endogenous polynucleotide that results in an altered amount of production of the encoded polypeptide—for example, an exogenous polynucleotide that increases the expression of an endogenous polypeptide—or a cell that in its native state does not produce the polypeptide. The increased production of a polypeptide of the invention is also referred to herein as overexpression. An exogenous polynucleotide of the invention includes polynucleotides that have not been separated from other components of the transgenic (recombinant) cell, or cell-free expression system, in which it is present, and polynucleotides produced in such cells or cell-free systems that are subsequently purified from at least some other components.The exogenous polynucleotide (nucleic acid) can be a contiguous stretch of nucleotides existing in nature, or comprise two or more contiguous stretches of nucleotides from different sources (of natural and / or synthetic origin) joined together. QAfrQQn / 1 znz / q / YILI form a single polynucleotide. Typically, such chimeric polynucleotides comprise at least one open reading frame encoding a polypeptide of the invention operatively linked to a promoter suitable for driving transcription of the open reading frame in a cell of interest. The percent identity of a polynucleotide is determined by GAP analysis (Needleman and Wunsch, 1970) (GCG program) with a gap creation penalty of 5 and a gap extension penalty of 0.3. The query sequence is at least 450 nucleotides long, and the GAP analysis aligns the two sequences in a region of at least 450 nucleotides. Preferably, the query sequence is at least 1,500 nucleotides long, and the GAP analysis aligns the two sequences in a region of at least 1,500 nucleotides. Even more preferably, the query sequence is at least 2,700 nucleotides long, and the GAP analysis aligns the two sequences in a region of at least 2,700 nucleotides. Even more preferably, the GAP analysis aligns two sequences along their entire length. With regard to the defined polynucleotides, it will be appreciated that higher % identity figures than those provided above will encompass preferred embodiments. Therefore, where appropriate, in light of the minimum % identity figures, it is preferred that the polynucleotide comprise a polynucleotide sequence that is at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 91%, more preferably at least 92%, more preferably at least 93%, more preferably at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, more preferably at least 99%, more preferably at least 99.1%, more preferably at least 99.2%, more preferably at least 99.3%, more preferably at least 99.4%, and more preferably at least 99.5%, more preferably at least 99.6%, more preferably at least 99.7%, more preferably at least 99.8%, and even more preferably at least 99.9% identical to the relevant SEQ ID NO. named. In a further embodiment, the present invention relates to polynucleotides that are substantially identical to those specifically described herein. As used herein, with reference to a polynucleotide, the term "substantially identical" means the substitution of one or a few (e.g., 2, 3, or 4) nucleotides while at least some activity of the native protein encoded by the polynucleotide is maintained. Furthermore, this term includes the addition or deletion of nucleotides that results in an increase or decrease in the size of the native protein encoded by one or a few (e.g., 2, 3, or 4) amino acids while at least some activity of the native protein encoded by the polynucleotide is maintained. QAfrQQn / Lznz / q / ΥΙΛΙ The present invention also relates to the use of oligonucleotides, for example, in methods for screening a polynucleotide of, or encoding a polypeptide of, the invention. As used herein, oligonucleotides are polynucleotides up to 50 nucleotides in length. The minimum size of such oligonucleotides is the size required for the formation of a stable hybrid between an oligonucleotide and a complementary sequence in a nucleic acid molecule of the present invention. They may be RNA, DNA, or combinations or derivatives thereof. Oligonucleotides are typically relatively short, single-stranded molecules of 10 to 30 nucleotides, commonly 15 to 25 nucleotides in length.When used as a guide for genome editing, a probe, or a primer in an amplification reaction, the minimum size of such an oligonucleotide is the size required for the formation of a stable hybrid between the oligonucleotide and a complementary sequence in a target nucleic acid molecule. Preferably, the oligonucleotides are at least 15 nucleotides long, more preferably at least 18 nucleotides, more preferably at least 19 nucleotides, more preferably at least 20 nucleotides, more preferably at least 22 nucleotides, and even more preferably at least 25 nucleotides long. The oligonucleotides of the present invention used as probes are typically conjugated to a tag such as a radioisotope, an enzyme, biotin, a fluorescent molecule, or a chemiluminescent molecule. Examples of oligonucleotides of the invention include those provided in SEQ IDs 30 and 31. The present invention includes oligonucleotides that can be used, for example, as guides for RNA-guided endonucleases, probes for identifying nucleic acid molecules, or primers for producing nucleic acid molecules. Probes and / or primers can be used to clone homologs of the polynucleotides of the invention from other species. Furthermore, hybridization techniques known in the art can also be used to screen genomic or cDNA libraries for such homologs. The polynucleotides and oligonucleotides of the present invention include those that hybridize under rigorous conditions with one or more of the sequences provided as SEQ ID NO: 2. As used herein, rigorous conditions are those that (1) employ low ionic strength and high washing temperature, for example, 0.015 M NaCl / 0.0015 M sodium citrate / 0.1% NaDodSO4 at 50°C; (2) employ during hybridization a denaturing agent such as formamide, for example, 50% (vol / vol) formamide with 0.1% bovine serum albumin, 0.1% Ficoll, 0.1% polyvinylpyrrolidone, 50 mM sodium phosphate buffer at pH 6.5 with 750 mM NaCl, 75 mM sodium citrate at 42°C; or (3) employ 50% formamide, 5 x SSC (0.75 M NaCl, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate, 5 x Denhardt's solution, sonicated salmon sperm DNA (50 g / ml), 0.1% SDS and 10% dextran sulfate at 42°C in 0.2 x SSC and 0.1% SDS. QAfrQQn / Lznz / q / ΥΙΛΙ The polynucleotides of the present invention may possess, when compared to naturally occurring molecules, one or more mutations that are deletions, insertions, or substitutions of nucleotide residues. The mutants may be of natural origin (i.e., isolated from a natural source) or synthetic (e.g., by performing site-directed mutagenesis in nucleic acid). A variant of a polynucleotide or oligonucleotide of the invention includes molecules of different sizes and / or is capable of hybridizing with the wheat genome close to that of the reference polynucleotide or oligonucleotide molecules defined herein. For example, the variants may comprise additional nucleotides (such as 1, 2, 3, 4, or more) or fewer nucleotides, provided they still hybridize with the target region. Furthermore, some nucleotides may be substituted without affecting the oligonucleotide's ability to hybridize with the target region.Furthermore, variants that hybridize close to, for example, within 50 nucleotides of, the region of the plant genome where the specific oligonucleotides defined herein hybridize can be easily engineered. In particular, this includes polynucleotides that encode the same polypeptide or amino acid sequence but vary in nucleotide sequence due to redundancy in the genetic code. The terms polynucleotide variant and variant also include naturally occurring allelic variants. Nucleic acid constructs The present invention includes nucleic acid constructs comprising the polynucleotides of the invention, vectors and host cells containing them, methods for their production and use, and uses thereof. The present invention relates to elements that are operatively joined or linked. Operationally joined or linked and the like refer to a linking of polynucleotide elements in a functional relationship. Typically, operatively joined nucleic acid sequences are linked contiguously and, when necessary to join two protein-coding regions, are contiguous and in the reading frame. One coding sequence is operatively linked to another coding sequence when RNA polymerase transcribes the two coding sequences into a single RNA molecule, which, if translated, is then translated into a single polypeptide having amino acids derived from both coding sequences.The coding sequences do not need to be contiguous with each other as long as the expressed sequences are ultimately processed to produce the desired protein. As used herein, the term cis-acting sequence, cis-acting element, cis-regulatory region, or a similar term shall be deemed to mean any nucleotide sequence which, when appropriately positioned and bound with respect to an expressible genetic sequence, is capable of regulating, at least in part, the QAfrQQn / L7n7 / 3 / YILI expression of the genetic sequence. Those skilled in the art will know that a cis regulatory region may be able to activate, silence, enhance, repress, or otherwise alter the level of expression and / or cell type specificity and / or developmental specificity of a genetic sequence at the transcriptional or post-transcriptional level. In preferred embodiments of the present invention, the cis-acting sequence is an activating sequence that enhances or stimulates the expression of an expressible genetic sequence. To operationally link a promoter or enhancer element to a transcribable polynucleotide means to place the transcribable polynucleotide (e.g., a protein-coding polynucleotide or other transcript) under the regulatory control of a promoter, which then controls the transcription of that polynucleotide. In constructing heterologous promoter / structural gene combinations, it is generally preferred to place a promoter, or a variant thereof, at a distance from the transcription start site of the transcribable polynucleotide that is approximately the same as the distance between that promoter and the protein-coding region it controls in its natural environment—that is, the gene from which the promoter is derived. As is known in the art, some variation in this distance can be accommodated without loss of function. Similarly, the preferred positioning of a regulatory sequence element (e.g., an operator, enhancer, etc.) is also considered.) with respect to a transcribable polynucleotide that will be placed under its control is defined by the positioning of the element in its natural environment; that is, the genes from which it is derived. Promoter, or promoter sequence as used herein, refers to a region of a gene, usually upstream (5') of the RNA-coding region, that controls the initiation and level of transcription in the cell of interest. A promoter includes the transcriptional regulatory sequences of a classic genomic gene, such as the TATA and CCAAT sequences, as well as additional regulatory elements (i.e., upstream activator sequences, enhancers, and silencers) that alter gene expression in response to developmental and / or environmental stimuli, or in a tissue- or cell-type-specific manner. A promoter is normally, but not necessarily (e.g., some Pollll promoters), located upstream of a structural gene whose expression it regulates. Furthermore, the regulatory elements comprising a promoter are typically located within 2 kb of the gene's transcription start site.Promoters may contain additional specific regulatory elements, located more distal to the start site to further enhance expression in a cell, and / or to alter the timing or inducibility of the expression of a structural gene to which it is operatively linked. A constitutive promoter refers to a promoter that directs the expression of an operatively linked transcribed sequence in many or all tissues of an organism, such as a QAfrQQn / 1 znz / q / YILI plant. The term constitutive, as used herein, does not necessarily indicate that a gene is expressed at the same level in all cell types, but rather that the gene is expressed in a wide range of cell types, although some variation in level is often detected. Selective expression, as used herein, refers to expression almost exclusively in specific organs of, for example, the plant, such as, for example, the endosperm, embryo, leaves, fruit, tubers, or root. In a preferred embodiment, a promoter is expressed selectively or preferentially in the leaves and / or stems of a plant, preferably a cereal plant. Selective expression may thus be contrasted with constitutive expression, which refers to expression in many or all tissues of a plant under most or all conditions experienced by the plant. Selective expression can also result in the compartmentalization of gene expression products into specific plant tissues, organs, or developmental stages, such as adults or seedlings. Compartmentalization into specific subcellular locations, such as the plastid, cytosol, vacuole, or apoplastic space, can be achieved by incorporating appropriate signals, such as a signal peptide, into the gene product structure for transport to the required cellular compartment. In the case of semiautonomous organelles (plastids and mitochondria), it can be achieved by integrating the transgene with appropriate regulatory sequences directly into the organelle's genome. A tissue-specific or organ-specific promoter is a promoter that is preferentially expressed in one tissue or organ relative to many other tissues or organs—preferably most, if not all, other tissues or organs in, for example, a plant. Typically, the promoter is expressed at a level 10 times higher in the specific tissue or organ than in other tissues or organs. In one modality, the promoter is a stem-specific promoter, a leaf-specific promoter, or a promoter that directs gene expression in an aerial part of the plant (at least stems and leaves) (green tissue-specific promoter) such as a ribulose-1,5-bisphosphate carboxylase oxygenase (RUBISCO) promoter. Examples of stem-specific promoters include, but are not limited to, those described in US 5,625,136 and Bam et al. (2008). The promoters contemplated by the present invention may be native to the host plant to be transformed or may be derived from an alternative source, where the region is functional in the host plant. Other sources include Agrobacterium T-DNA genes, such as gene promoters for the biosynthesis of nopalin, octapin, mannopin, or other opin promoters; tissue-specific promoters (see, for example, US 5,459,252 and WO 91 / 13992); viral promoters (including host-specific viruses); or partial promoters. QAfrQQn / 1 znz / q / YILI or totally synthetic. Numerous promoters that are functional in mono- and dicotyledonous plants are well known in the art (see, for example, Greve, 1983; Solomon et al., 1984; Garfinkel et al., 1983; Barker et al., 1983); including several promoters isolated from plants and viruses such as the cauliflower mosaic virus promoter (CaMV 35S, 19S). Medberry et al. describe non-limiting methods for evaluating promoter activity (1992, 1993), Sambrook et al. (1989, supra) and US 5,164,316. Alternatively or additionally, the promoter may be an inducible promoter or a developmentally regulated promoter capable of directing the expression of the introduced polynucleotide at an appropriate developmental stage of the plant, for example. Other sequences that act in c / s that may be employed include transcriptional and / or translational enhancers. Enhancer regions are well known to those skilled in the art and may include an ATG translation initiation codon and adjacent sequences. When included, the initiation codon must be in phase with the reading frame of the coding sequence related to the foreign or exogenous polynucleotide to ensure translation of the entire sequence if it is to be translated. Translation initiation regions may be provided from the source of the transcription initiation region or from a foreign or exogenous polynucleotide.The sequence can also be derived from the source of the selected promoter to drive transcription, and can be specifically modified to increase mRNA translation. The nucleic acid construct of the present invention may comprise a 3' untranslated sequence of approximately 50 to 1000 nucleotide base pairs, which may include a transcription termination sequence. A 3' untranslated sequence may contain a transcription termination signal, which may or may not include a polyadenylation signal and any other regulatory signal capable of effecting mRNA processing. A polyadenylation signal functions for the addition of polyadenylic acid tracts to the 3' end of an mRNA precursor. Polyadenylation signals are commonly recognized by the presence of homology to the canonical form 5' AATAAA-3', although variations are not uncommon. Transcription termination sequences that do not include a polyadenylation signal include terminators for the RNA polymerase Poly or Poll1, comprising a series of four or more thymidines.Examples of suitable 3' untranslated sequences are the 3' untranslated transcribed regions containing a polyadenylation signal from an octopine synthase (oes) or nopaline synthase (nos) gene from Agrobacterium tumefaciens (Bevan et al., 1983). Suitable 3' untranslated sequences can also be derived from plant genes such as the ribulose-1,5-bisphosphate carboxylase (ssRUBISCO) gene, although other 3' elements known to those skilled in the technique may also be used. QAfrQQn / L7n7 / 3 / YILI Since the DNA sequence inserted between the transcription start site and the start of the coding sequence—that is, the 5' untranslated leader sequence (5'UTR)—can influence gene expression if it is translated and transcribed, a particular leader sequence can also be employed. Suitable leader sequences include those that comprise sequences selected to direct the optimal expression of the foreign or endogenous DNA sequence. For example, such leader sequences include a preferred consensus sequence that can increase or maintain mRNA stability and prevent inappropriate translation initiation, as described by Joshi (1987). Vectors The present invention includes the use of vectors for the manipulation or transfer of genetic constructs. A chimeric vector is understood to be a nucleic acid molecule, preferably a DNA molecule derived, for example, from a plasmid, bacteriophage, or plant virus, into which a nucleic acid sequence can be inserted or cloned. A vector is preferably double-stranded DNA and contains one or more unique restriction sites and may be capable of autonomous replication in a defined host cell, which includes a target cell or tissue or a precursor cell or tissue thereof, or capable of integrating into the genome of the defined host such that the cloned sequence is reproducible.Consequently, the vector can be a self-replicating vector, meaning a vector that exists as an extrachromosomal entity whose replication is independent of chromosomal replication—for example, a closed linear or circular plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means to ensure self-replication. Alternatively, the vector may be one that, when introduced into a cell, integrates into the recipient cell's genome and replicates along with the chromosome or chromosomes into which it has integrated. A vector system may comprise a single vector or plasmid, two or more vectors or plasmids that together contain the total DNA to be introduced into the host cell's genome, or a transposon. The choice of vector will typically depend on the vector's compatibility with the cell into which it will be introduced.The vector may also include a selection marker such as an antibiotic resistance gene, a herbicide resistance gene, or another gene that can be used to select suitable transformants. Experts in the technique are familiar with examples of such genes. The nucleic acid construct of the invention can be introduced into a vector, such as a plasmid. Plasmid vectors typically include additional nucleic acid sequences that facilitate the selection, amplification, and transformation of the expression cassette in prokaryotic and eukaryotic cells, for example, pUC-derived vectors, pSK-derived vectors, QRbQQn / 1707 / 3 / YILI pGEM-derived vectors, pSP-derived vectors, pBS-derived vectors, or binary vectors containing one or more T-DNA regions. Additional nucleic acid sequences include origins of replication to provide autonomous replication of the vector, selectable marker genes, preferably encoding antibiotic or herbicide resistance, unique multiple cloning sites providing multiple sites for inserting nucleic acid sequences or genes encoded in the nucleic acid construct, and sequences that enhance the transformation of prokaryotic and eukaryotic cells (especially plants). A marker gene is a gene that imparts a distinct phenotype to cells expressing the marker gene and thus allows such transformed cells to be distinguished from cells lacking the marker. A selectable marker gene confers a trait for which selection can be made based on resistance to a selective agent (e.g., a herbicide, antibiotic, radiation, heat, or other treatment that damages non-transformed cells). A cridible marker gene (or reporter gene) confers a trait that can be identified by observation or testing, i.e., by screening (e.g., β-glucuronidase, luciferase, GFP, or other enzymatic activity not present in non-transformed cells). The marker gene and the nucleotide sequence of interest do not have to be linked. To facilitate the identification of transformants, the nucleic acid construct desirably comprises a selectable or critical marker gene as, or in addition to, the foreign or exogenous polynucleotide. The actual choice of a marker is not crucial as long as it is functional (i.e., selective) in combination with the plant cells of choice. The marker gene and the foreign or exogenous polynucleotide of interest do not have to be linked, since cotransformation of unlinked genes, as described in US 4,399,216, is also an effective process in plant transformation. Examples of selectable DNA markers are markers that confer resistance to antibiotics such as resistance to ampicillin, erythromycin, chloramphenicol or tetracycline, preferably resistance to kanamycin.Selectable markers for plant transformant selection include, but are not limited to, a hig gene encoding resistance to hygromycin B; a neomycin phosphotransferase (nptll) gene conferring resistance to kanamycin, paromomycin, G418; a rat liver glutathione-S-transferase gene conferring resistance to glutathione-derived herbicides as, for example, described in EP 256223; a glutamine synthetase gene conferring, upon overexpression, resistance to glutamine synthetase inhibitors such as phosphinothicin as, for example, described in WO 87 / 05327; a Streptomyces viridochromogenes acetyltransferase gene conferring resistance to the selective agent phosphinothicin as, for example, described in EP 275957; and a gene. QAfrQQn / 1 znz / q / YILI encoding a 5-enolshikimate-3-phosphate synthase (EPSPS) conferring tolerance to N-phosphonomethylglycine as, for example, described by Hinchee et al. (1988); a bar gene conferring resistance to bialofos as, for example, described in WO91 / 02071; a nitrilase gene such as bxn from Klebsiella ozaenae conferring resistance to bromoxynil (Stalker et al., 1988); a dihydrofolate reductase (DHFR) gene conferring resistance to methotrexate (Thillet et al., 1988); a mutating acetolactate synthase (ALS) gene conferring resistance to imidazolinone, sulfonylurea, or other ALS-inhibiting chemicals (EP 154,204); a mutated anthranilate synthase gene that confers resistance to 5-methyl tryptophan; or a dalapon dehalogenase gene that confers resistance to the herbicide. Preferred screening markers include, among others, a uidA gene encoding a β-glucuronidase (GUS) enzyme for which several chromogenic substrates are known; a β-galactosidase gene encoding an enzyme for which chromogenic substrates are known; an aequorin gene (Prasher et al., 1985), which can be used in the detection of calcium-sensitive bioluminescence; a green fluorescent protein gene (Niedz et al., 1995) or derivatives thereof; a luciferase (luc) gene (Ow et al., 1986), which allows for the detection of bioluminescence; and others known to the technique. A reporter molecule, as used herein, is understood to be a molecule that, by its chemical nature, provides an analytically identifiable signal that facilitates the determination of promoter activity by reference to the protein product. Preferably, the nucleic acid construct is stably incorporated into the genome of, for example, a plant. Accordingly, the nucleic acid comprises appropriate elements that allow the molecule to be incorporated into the genome, or the construct is placed in an appropriate vector that can be incorporated into a chromosome of a plant cell. One embodiment of the present invention includes a recombinant vector, comprising at least one polynucleotide molecule of the present invention, inserted into any vector capable of delivering the nucleic acid molecule to a host cell. This vector contains heterologous nucleic acid sequences, i.e., nucleic acid sequences not found naturally alongside the nucleic acid molecules of the present invention and preferably derived from a species other than the species from which the nucleic acid molecule or molecules are derived. The vector may be RNA or DNA, prokaryotic or eukaryotic, and is typically a virus or a plasmid. Several vectors suitable for stable transfection of plant cells or for the establishment of transgenic plants have been described in, for example, Pouwels et al., Cloning Vectors: A Laboratory Manual, 1985, suppl. 1987; Weissbach and Weissbach, Methods for Plant Molecular Biology, Academic Press, 1989; and Gelvin et al., Plant Molecular Biology Manual, Kluwer QRbQQn / 1707 / 3 / YILI Academic Publishers, 1990. Typically, plant expression vectors include, for example, one or more cloned plant genes under the transcriptional control of 5' and 3' regulatory sequences and a selectable dominant marker. Such plant expression vectors may also contain a promoter regulatory region (e.g., a regulatory region that controls inducible or constitutive, environmentally or developmentally regulated, or tissue- or cell-specific expression), a transcription start site, a ribosome binding site, an RNA processing signal, a transcription termination site, and / or a polyadenylation signal. The level of a protein of the invention can be modulated by increasing the expression level of a nucleotide sequence encoding the protein in a plant cell, or by decreasing the expression level of a gene encoding the protein in the plant, leading to modified pathogen resistance. The expression level of a gene can be modulated by altering the number of copies per cell, for example, by introducing a synthetic genetic construct comprising the coding sequence and a transcriptional control element that is operatively linked to it and functional in the cell. A plurality of transformants can be selected and screened for those with a favorable level and / or specificity of transgenic expression arising from the influence of endogenous sequences in the vicinity of the transgenic integration site.A favorable level and pattern of transgenic expression is one that results in a substantial modification of pathogen resistance or another phenotype. Alternatively, a mutagenized seed population or a plant population from a breeding program can be selected for individual lines with altered pathogen resistance or another phenotype associated with pathogen resistance. Recombinant cells Another embodiment of the present invention includes a recombinant cell comprising a host cell transformed with one or more recombinant molecules of the present invention, or cells derived therefrom. The transformation of a nucleic acid molecule into a cell can be carried out by any method by which a nucleic acid molecule can be inserted into the cell. Transformation techniques include, but are not limited to, transfection, particle bombardment / biolistics, electroporation, microinjection, lipofection, adsorption, and protoplast fusion. In one embodiment, gene editing is used to transform the target cell using, for example, targeted nucleases such as TALEN or Cas9CRISPR. A recombinant cell can remain unicellular or can develop into a tissue, organ, or multicellular organism. The transformed nucleic acid molecules of the present The QAfrQQn / 1 znz / q / YILI invention may remain extrachromosomal or may be integrated into one or more sites within a chromosome of the transformed (i.e., recombinant) cell in such a way that their ability to be expressed is preserved. The preferred host cells are plant cells, more preferably cells from a cereal plant, more preferably barley or wheat cells, and even more preferably a wheat cell. qenoma edition Endonucleases can be used to generate single-strand or double-strand breaks in genomic DNA. Genomic DNA breaks in eukaryotic cells are repaired using non-homologous end joining (NHEJ) pathways or homology-directed repair (HDR). NHEJ can result in imperfect repair, leading to unintended mutations, while HDR can allow for precise gene insertion using an exogenously supplied repair DNA template. CRISPR-associated proteins (Cas) have received significant interest, and although transcription activator-like effector nucleases (TALENs) and zinc finger nucleases remain useful, the CRISPR-Cas system offers a simpler, more versatile, and less expensive tool for genome editing (Doudna and Charpentier, 2014). CRISPR-Cas systems are classified into three main groups that utilize various nucleases or combinations of nucleases. In class 1 CRISPR-Cas systems (types I, III, and IV), the effector module consists of a multi-protein complex, while class 2 systems (types II, V, and VI) use only a single effector protein (Makarova et al., 2015). Cas includes a gene that is coupled to, near, or located close to flanking CRISPR loci. Haft et al. (2005) provides a review of the Cas protein family. The nuclease is guided by a synthetic small guide RNA (gRNA), which may or may not include tracRNA, resulting in a simplification of the CRISPR-Cas system to two genes: the endonuclease and the gRNA (Jinek et al., 2012). The gRNA is typically under the regulatory control of a U3 or U6 nuclear small RNA promoter. The gRNA recognizes the specific gene and targets a portion of it. The protospacer adjacent motif (PAM) is adjacent to the target site, which limits the number of potential CRISPR-Cas targets in a genome, although nuclease expansion also increases the number of available PAMs. There are numerous web tools available for designing gRNAs, including CHOPCHOP (http: / / chopchop.cbu.uib.no), CRISPR design https: / / omictools.com / crispr-design-tool, E-CRISP http: / / www.e-crisp.org / E-CRISP / , Geneious or Benchling https: / / benchling.com / crispr. CRISPR-Cas systems are the most frequently adopted in eukaryotic work to date, using a Cas9 effector protein that is generally used by Streptococcus QAfrQQn / I 7P7 / 3 / YILI pyogenes Cas9 guided by RNA or an optimized sequence variant in multiple plant species (Luo et al., 2016). Luo et al. (2016) summarizes numerous studies in which genes in various plant species have been successfully targeted to induce indels and loss-of-function mutant phenotypes in the open reading frame of the endogenous gene and / or promoter. Due to the cell wall in plant cells, the delivery of the CRISPR-Cas machinery into the cell and successful transgenic regenerations have utilized Agrobacterium tumefaciens infection (Luo et al., 2016), plasmid DNA particle bombardment, or biolistic delivery. Suitable vectors for cereal transformation include pCXUNcas9 (Sun et al, 2016) or pYLCRISPR / Cas9Pubi-H available from Addgene (Ma et al., 2015, accession number KR029109.1). Alternative CRISPR-Cas systems refer to effector enzymes that contain the RuvC nuclease domain but not the HNH domain, including the Cas12 enzymes (Cas12a, Cas12b, Cas12f), Cpf1, C2c1, and C2c3. Cpf1 creates staggered double-strand breaks at the distal position of PAM, and its smaller size may provide advantages for certain species (Begemann et al., 2017). Other CRISPR-Cas systems include RNA-guided RNases such as Cas13, Cas13a (C2c2), Cas13b, and Cas13c. QAfrQQn / 1 znz / q / YILI Sequence insertion or integration The CRISPR-Cas system can be combined with the provision of a nucleic acid sequence to direct homology-directed repair for the insertion of a sequence into a genome. Genome-directed integration of plant transgenes allows the sequential addition of transgenes at the same locus. This cis-gene stacking would greatly simplify subsequent breeding efforts, with all inherited transgenes appearing as a single locus. When combined with CRISPR / Cas9, the transgene target site excision can be incorporated into this locus via homology-directed repair facilitated by flanking sequence homology. This approach can be used to rapidly introduce new alleles without linkage carryover or to introduce naturally occurring allelic variants. Nickasas CRISPR-Cas II systems utilize a Cas9 nuclease with two enzyme cleavage domains: a RuvC domain and an HNH domain. Mutations have been shown to alter the double-stranded cleavage to a single-stranded cleavage, resulting in a technology variant called nickase or nuclease-inactivated Cas9. The RuvC subdomain cleaves the strand of Non-complementary DNA and the HNH subdomain cleave that DNA strand complementary to the gRNA. Cas9 inactivated with nickases or nucleases retains the ability to bind to DNA directed by the gRNA. Mutations in the subdomains are known in the technique, for example, S. pyogenes Cas9 nuclease with a D10A mutation or an H840A mutation. Editing or modification of the genome base Base editors have been created by fusing a deaminase with a Cas9 domain (WO 2018 / 086623). By fusing the deaminase, the gRNA-directed sequence can be used to perform the conversion of cytidine (C) to uracil (U) by deamination of cytidine in DNA. The cell's mismatch repair mechanisms then replace the U with a T. Suitable cytidine deaminases may include APOBEC1 deaminase, activation-induced cytidine deaminase (AID), APOBEC3G, and CDA1. In addition, the Cas9-deaminase fusion can be a mutated Cas9 with nickase activity to generate a single-strand break. It has been suggested that the nickase protein is potentially more efficient at promoting homology-directed repair (Luo et al., 2016). Vector-free genome editing or genome modification More recent methods for using vector-free approaches with Cas9 ribonucleoproteins / guRNA have been described, successfully reducing off-target events. The method requires in vitro expression of Cas9 ribonucleoproteins (RNPs) that are transformed in the cell or protoplast and does not depend on Cas9 integration into the host genome, thus reducing undesirable sidecuts that have been associated with random Cas9 gene integration. Only short flanking sequences are required to form a stable Cas9 and a stable guRNA ribonucleoprotein in vitro. Woo et al. (2015) introduced pre-assembled Cas9 / guRNA protein / RNA complexes into Arabidopsis, rice, lettuce, and tobacco protoplasts, and observed site-directed mutagenesis frequencies of up to 45% in regenerated plants. RNP and in vitro demonstrated in several species, including dicotyledonous plants (Woo et al., 2015), and monocotyledonous maize (Svitashev et al., 2016) and wheat (Liang et al., 2017). Plant genome editing using in vitro CRISPRCas 9 transcripts or ribonucleoproteins is fully described in Liang et al. (2018) and Liang et al. (2019). Gene insertion method Plant embryos can be bombarded with a Cas9 gene and a RNAgu gene that target the integration site along with the DNA repair template. The templates of DNA repair agents can be a synthesized DNA fragment or a 127-mer oligonucleotide, each encoding the cDNA or the gene of interest. The bombarded cells are cultured in tissue culture medium. DNA extracted from callus or leaf tissue of T0 plants using the CTAB DNA extraction method can be analyzed by PCR to confirm gene integration. Selected T1 plants are then tested to confirm the presence of the gene of interest. The method involves introducing the DNA sequence of interest, called donor DNA, and an endonuclease into a plant cell. The endonuclease creates a break at the target site, allowing the first and second homology regions of the donor DNA to undergo homologous recombination with their corresponding genomic homology regions. The cut genomic DNA acts as an acceptor for the DNA sequence. The resulting exchange of DNA between the donor and the plant genome leads to the integration of the polynucleotide of interest from the donor DNA into the strand break at the target site in the plant genome, thereby altering the original target site and producing an altered genomic sequence. Donor DNA can be introduced by any known means. For example, a plant with a target site is provided. Donor DNA can be delivered to the plant using known transformation methods, including Agrobacterium-mediated transformation or biolistic particle bombardment. The RNA-guided endonuclease Cas or Cpf1 cleaves the DNA at the target site, and the donor DNA is inserted into the genome of the transformed plant. Although homologous recombination occurs infrequently in plant somatic cells, the process appears to be enhanced / stimulated by the introduction of double-strand breaks (DSBs) at selected endonuclease target sites. Ongoing efforts to generate Cas, particularly Cas9, variants, or alternatives such as Cpf1 or Cms1 may improve efficiency. Transgenic plants The term "plant," as used herein as a noun, refers to whole plants and any member of the Kingdom Plantae. When used as an adjective, it refers to any substance present in, obtained from, derived from, or related to a plant, such as plant organs (e.g., leaves, stems, roots, flowers), individual cells (e.g., pollen), seeds, plant cells, and the like. Seedlings and germinated seeds from which roots and shoots have arisen are also included within the meaning of "plant." The term "plant parts," as used herein, refers to one or more plant tissues or organs obtained from a plant and comprising plant genomic DNA. Plant parts include vegetative structures (e.g., leaves, stems), roots, floral organs / structures, seeds (including the embryo, cotyledons, and seed coat), and other tissues. QAfrQQn / L7n7 / 3 / YILI of plants (for example, vascular tissue, ground tissue, and the like), cells, and their offspring. The term "plant cell" as used herein refers to a cell obtained from or in a plant and includes protoplasts or other plant-derived cells, gamete-producing cells, and cells that regenerate into whole plants. Plant cells may be cells in culture. Plant tissue means differentiated tissue in or obtained from a plant (explant) or undifferentiated tissue derived from immature or mature embryos, seeds, roots, shoots, fruits, tubers, pollen, tumor tissue such as crown tumors, and various forms of aggregates of plant cells in culture, such as calluses. Exemplary plant tissues in or from seeds are the cotyledon, the embryo, and the embryo axis. Accordingly, the invention includes plants, parts of plants, and products comprising them. As used herein, the term seed refers to the mature seed of a plant, which is ready for harvest or has been collected from the plant, such as is typically harvested commercially in the field, or as developing seed that occurs in a plant after fertilization and before seed dormancy is established and before harvest. A transgenic plant, as used herein, refers to a plant that contains a nucleic acid construct not found in a wild-type plant of the same species, variety, or cultivar. That is, transgenic plants (transformed plants) contain genetic material (a transgene) that they did not contain before transformation. The transgene may include genetic sequences obtained from or derived from a plant cell or another plant cell, a non-plant source, or a synthetic sequence. Typically, the transgene is introduced into the plant through human manipulation, such as transformation, but any method recognized by a person skilled in the art may be used. The genetic material is preferably stably integrated into the plant genome.The introduced genetic material may include sequences that occur naturally in the same species but in a rearranged order or a different arrangement of elements, for example, an antisense sequence. Plants containing such sequences are included in the group present in transgenic plants. A non-transgenic plant is one that has not been genetically modified through the introduction of genetic material by human intervention, using, for example, recombinant DNA techniques. In a preferred embodiment, transgenic plants are homozygous for each and every gene that has been introduced (transgene) so that their offspring do not segregate for the desired phenotype. As used herein, the term compared to an isogenic plant, or similar phrases, refers to a plant that is isogenic in relation to the transgenic plant but without the QAfrQQn / L7n7 / 3 / YILI transgene of interest. Preferably, the corresponding non-transgenic plant is of the same cultivar or variety as the precursor of the transgenic plant of interest, or a sister plant line lacking the construct, often referred to as the segregant, or a plant of the same cultivar or variety transformed with an empty vector construct, and may be a non-transgenic plant. Wild type, as used herein, refers to a cell, tissue, or plant that has not been modified according to the invention. Wild type cells, tissues, or plants may be used as controls to compare the expression levels of an exogenous nucleic acid or the extent and nature of the trait modification with cells, tissues, or plants modified as described herein. Transgenic plants, as defined in the context of the present invention, include the offspring of plants that have been genetically modified using recombinant techniques, wherein the offspring comprise the transgene of interest. Such offspring may be obtained by self-fertilization of the primary transgenic plant or by crossing such plants with another plant of the same species. Generally, this would be to modulate the production of at least one defined protein present in the desired plant or plant organ. Transgenic plant parts include all parts and cells of such plants that comprise the transgene, such as, for example, cultured tissues, calluses, and protoplasts. The plants contemplated for use in the practice of the present invention include both monocots and dicots. The target plants include, among others, the following: cereals (e.g., wheat, barley, rye, oats, rice, corn, sorghum, and related crops); grapes; beets (sugar beets and fodder beets); pome fruits, stone fruits, and berries (apples, pears, plums, peaches, almonds, cherries, strawberries, raspberries, and blackberries); legumes (beans, lentils, peas, soybeans); oilseeds (rapeseed or other Brassicas, mustard, poppy, olives, sunflowers, safflower, flax, coconut, castor beans, cocoa beans, peanuts); cucumber plants (zucchini, cucumbers, melons); and fiber plants (cotton, flax, hemp, jute). citrus fruits (oranges, lemons, grapefruits, tangerines); vegetables (spinach, lettuce, asparagus, cabbage, carrots, onions, tomatoes, potatoes, paprika); laurel fruits (avocados, cinnamon, camphor);or plants such as corn, tobacco, nuts, coffee, sugarcane, tea, vines, hops, turfgrass, bananas, and natural rubber plants, as well as ornamentals (flowers, shrubs, broadleaf and perennial, such as conifers). Preferably, the plant is a cereal plant, more preferably wheat, rice, corn, triticale, oats, or barley, even more preferably wheat. As used herein, the term wheat refers to any species of the genus Triticum, including its ancestors, as well as its offspring produced by crosses with other species. Wheat includes hexaploid wheat, which has a genomic organization of AABBDD, consisting of 42 chromosomes, and tetraploid wheat, which has a genomic organization of QAfrQQn / L7n7 / 3 / YILI AABB, composed of 28 chromosomes. Hexaploid wheat includes T. aestivum, T. spelta, T. macha, T. compactum, T. sphaerococcum, T. vavilovii, and crosses between these species. A preferred species of hexaploid wheat is T. aestivum ssp. aestivum (also called bread wheat). Tetraploid wheat includes T. durum (also referred to herein as durum wheat or Triticum turgidum ssp. durum), T. dicoccoides, T. dicoccum, T. polonicum, and crosses between these species. Furthermore, the term wheat includes potential precursors of Triticum sp. hexaploid or tetraploid such as T. uartu, T. monococcum or T. boeoticum for genome A, Aegilops speltoides for genome B and T. tauschii (also known as Aegilops squarrosa or Aegilops tauschii) for genome D. The particularly preferred precursors are those of genome A, even more preferably the precursor of genome A is T. monococcum.A wheat crop for use in the present invention may belong to, but is not limited to, any of the species listed above. Also included are plants produced by conventional techniques using Triticum sp. as a parent in a sexual cross with a non-Triticum species (such as rye [Secale cereale]), including, but not limited to, Triticale. As used herein, the term barley refers to any species of the genus Hordeum, including its ancestors, as well as its offspring produced by crosses with other species. Preference is given to the plant being of a Hordeum species that is commercially cultivated, such as a strain, cultivar, or variety of Hordeum vulgare, or one that is suitable for commercial grain production. Transgenic plants, as defined in the context of the present invention, include plants (as well as parts and cells thereof) and their offspring that have been genetically modified using recombinant techniques to induce the production of at least one polypeptide of the present invention in the desired plant or plant organ. Transgenic plants can be produced using techniques known in the art, such as those generally described in A. Slater et al., Plant Biotechnology - The Genetic Manipulation of Plants, Oxford University Press (2003), and P. Christou and H. Klee, Handbook of Plant Biotechnology, John Wiley and Sons (2004). In a preferred embodiment, transgenic plants are homozygous for each and every one of the introduced genes (transgenes) so that their offspring do not segregate for the desired phenotype. Transgenic plants can also be heterozygous for the introduced transgene or transgenes, as, for example, in F1 offspring grown from hybrid seeds. Such plants can provide advantages such as hybrid vigor, which is well known in the art. As used herein, other genetic markers can be any molecule that is linked to a desired trait in a plant. Such markers are well QAfrQQn / 1 znz / q / YILI are known to experts in the technique and include molecular markers linked to genes that determine traits such as disease resistance, yield, plant morphology, grain quality, dormancy traits, grain color, gibberellic acid content in the seed, plant height, flour color, and the like. Examples of such genes are the stripe rust resistance genes Yr10 or Yr17, nematode resistance genes such as Crei and Cre3, alleles at glutenin loci that determine dough strength such as the Ax, Bx, Dx, Ay, By, and Dy alleles, and Rht genes that determine a semi-dwarf growth habit and thus lodging resistance. Four general methods have been described for the direct delivery of a gene to cells: (1) chemical methods (Graham et al., 1973); (2) physical methods such as microinjection (Capecchi, 1980); electroporation (see, for example, WO 87 / 06614, US 5,472,869, 5,384,253, WO 92 / 09696 and WO 93 / 21335); and gene gun (see, for example, US 4,945,050 and US 5,141,131); (3) viral vectors (Clapp, 1993; Lu et al., 1993; Eglitis et al., 1988); and (4) receptor-mediated mechanisms (Curiel et al., 1992; Wagner et al., 1992). Acceleration methods that can be used include, for example, microprojectile bombardment and similar techniques. One example of a method for delivering transforming nucleic acid molecules to plant cells is microprojectile bombardment. This method has been reviewed by Yang et al., Particle Bombardment Technology for Gene Transfer, Oxford Press, Oxford, England (1994). Non-biological particles (microprojectiles) can be coated with nucleic acids and introduced into cells by a propulsive force. Exemplary particles include those composed of tungsten, gold, platinum, and similar materials. A particular advantage of microprojectile bombardment, besides being an efficient means of reproducibly transforming monocots, is that it does not require protoplast isolation or susceptibility to Agrobacterium infection.A suitable particle delivery system for use with the present invention is the PDS-1000 / He helium-accelerating gun available from Bio-Rad Laboratories. For bombardment, immature embryos or derived target cells such as scutellae or calli of immature embryos can be arranged in a solid culture medium. In another alternative modality, plastids can be stably transformed. The method described for the transformation of plastids in higher plants includes gun delivery of DNA particles containing a selectable marker and targeting the DNA to the plastid genome by homologous recombination (US 5,451,513, US 5,545,818, US 5,877,402, US 5,932479, and WO 99 / 05265). Agrobacterium-mediated transfer is a widely applicable system for introducing genes into plant cells because DNA can be introduced into whole plant tissues. QAfrQQn / 1 znz / q / YILI thus avoiding the need to regenerate an intact plant from a protoplast. The use of Agrobacterium-mediated plant integration vectors to introduce DNA into plant cells is well known in the art (see, for example, US 5,177,010, US 5,104,310, US 5,004,863, US 5,159,135). Furthermore, T-DNA integration is a relatively precise process that results in few transpositions. The region of DNA to be transferred is defined by the edge sequences, and the intervening DNA is generally inserted into the plant genome. Agrobacterium transformation vectors are capable of replicating in E. coli as well as in Agrobacterium, allowing for convenient manipulations as described (Klee et al., Plant DNA Infectious Agents, Hohn and Schell, (editors), Springer-Verlag, New York, (1985): 179-203). Furthermore, technological advances in vectors for Agrobacterium-mediated gene transfer have improved the arrangement of genes and restriction sites in the vectors to facilitate the construction of vectors capable of expressing multiple polypeptide-coding genes. The described vectors have convenient multilinker regions flanked by a promoter and a polyadenylation site for the direct expression of inserted polypeptide-coding genes and are suitable for the present purposes. In addition, Agrobacterium containing armed and disarmed Ti genes can be used for transformations.In those plant varieties where Agrobacterium-mediated transformation is efficient, it is the method of choice due to the easy and defined nature of gene transfer. A transgenic plant produced using Agrobacterium transformation methods typically contains a single genetic locus on a chromosome. Such transgenic plants can be referred to as hemizygous for the added gene. A transgenic plant that is homozygous for the added structural gene is more desirable; that is, a transgenic plant containing two added genes, one gene at the same locus on each chromosome of a chromosome pair. A homozygous transgenic plant can be obtained by sexually mating (self-fertilization) an independently segregating transgenic plant containing a single added gene, germinating some of the resulting seed, and testing the resulting plants for the gene of interest. It should also be understood that two different transgenic plants can be mated / crossed to produce offspring containing two independent segregating exogenous genes. Self-fertilization of the appropriate offspring can produce plants that are homozygous for both exogenous genes. Backcrossing with a parental plant and crossing with a non-transgenic plant are also considered, as is vegetative propagation. Descriptions of other breeding methods can be found elsewhere. QAfrQQn / L7n7 / 3 / YILI commonly for different traits and crops in Fehr, Breeding Methods for Cultivar Development, J. Wilcox (editor) American Society of Agronomy, Madison Wis. (1987). The transformation of plant protoplasts can be achieved using methods based on calcium phosphate precipitation, polyethylene glycol treatment, electroporation, and combinations of these treatments. The application of these systems to different plant varieties depends on the ability of that particular plant strain to regenerate from protoplasts. Illustrative methods for the regeneration of cereals from protoplasts are described (Fujimura et al., 1985; Toriyama et al., 1986; Abdullah et al., 1986). Other methods of cell transformation can also be used and include, among others, the introduction of polynucleotides such as DNA into plants by direct transfer to pollen, by direct injection of polynucleotides such as DNA into the reproductive organs of a plant, or by direct injection of polynucleotides such as DNA into the cells of immature embryos followed by rehydration of the desiccated embryos. The regeneration, development, and cultivation of plants from protoplast transformants of a single plant or from multiple transformed explants are well known in the field (Weissbach et al., Methods for Plant Molecular Biology, Academic Press, San Diego, (1988)). This regeneration and growth process generally includes the stages of selecting transformed cells, culturing these individual cells through the usual stages of embryonic development through the rooted seedling stage. Transgenic embryos and seeds are regenerated similarly. The resulting rooted transgenic shoots are then planted in an appropriate plant growth medium, such as soil. The development or regeneration of plants containing the foreign exogenous gene is well known in the art. Preferably, the regenerated plants are self-pollinated to produce homozygous transgenic plants. Alternatively, pollen obtained from the regenerated plants is crossed with plants grown from seeds of agronomically important lines. Conversely, pollen from plants of these important lines is used to pollinate the regenerated plants. A transgenic plant of the present invention containing a desired exogenous nucleic acid is grown using methods well known to those skilled in the art. Methods have been published for transforming dicotyledons, mainly through the use of Agrobacterium tumefaciens, and obtaining transgenic plants for cotton (US 5,004,863, US 5,159,135, US 5,518,908); soybeans (US 5,569,834, US 5,416,011); Brassica (US 5,463,174); peanuts (Cheng et al., 1996); and peas (Grant et al., 1995). Methods for transforming cereal plants such as wheat and barley to introduce genetic variation into the plant by introducing an exogenous nucleic acid and for regenerating plants from protoplasts or embryos of immature plants are QAfrQQn / L7n7 / 3 / YILI well known in the art, see, for example, CA 2,092,588, AU 61781 / 94, AU 667939, US 6,100,447, WO 97 / 048814, US 5,589,617, US 6,541,257 and other methods are set out in WO 99 / 14314. Preferably, transgenic wheat or barley plants are produced by Agrobacterium tumefaciens-mediated transformation procedures. Vectors carrying the desired nucleic acid construct can be introduced into regenerable wheat cells from plants or tissue culture explants, or suitable plant systems such as protoplasts. Regenerable wheat cells preferably come from the scutellum of immature embryos, from mature embryos, from calluses derived from them, or from meristematic tissue. To confirm the presence of transgenes in transgenic cells and plants, polymerase chain reaction (PCR) amplification or Southern blot analysis can be performed using methods familiar to experts in the technique. Transgene expression products can be detected in various ways, depending on the nature of the product, including Western blot and enzyme assays. A particularly useful way to quantify protein expression and detect replication in different plant tissues is to use a reporter gene, such as GUS. Once transgenic plants have been obtained, they can be cultured to produce tissues or plant parts with the desired phenotype. The plant tissue or plant parts can then be harvested, and / or the seeds collected.The seed can serve as a source for growing additional plants with tissues or parts that have the desired characteristics. Marker-assisted selection Marker-assisted selection is a well-recognized method for selecting heterozygous plants required when backcrossing with a recurrent parent in a classical breeding program. The plant population in each backcross generation will be heterozygous for the gene of interest, typically present in a 1:1 ratio in a backcross population, and a molecular marker can be used to distinguish the two alleles of the gene. By extracting DNA from, for example, young shoots and testing with a specific marker for the desirable introgressed trait, early selection of plants for further backcrossing is achieved while concentrating energy and resources on fewer plants.To further accelerate the backcrossing program, the embryo of immature seeds (25 days after anthesis) can be removed and cultured in nutrient media under sterile conditions, instead of allowing the seed to fully mature. This process, called embryo rescue, is used in combination with DNA extraction at the three-leaf stage and analysis for at least one Sr26 allele or variant that confers genetic trait to the plant. QAfrQQn / 1 znz / q / YILI resistance to at least one strain of Puccinia graminis, allows rapid selection of plants carrying the desired trait, which can be nurtured to maturity in the greenhouse or in the field for further backcrossing with the recurrent parent. The methods of the present invention may utilize any molecular biology technique known in the art. Such methods include, but are not limited to, nucleic acid amplification, nucleic acid sequencing, nucleic acid hybridization with appropriately labeled probes, single-strand conformational analysis (SSCA), denaturing gradient gel electrophoresis (DGGE), heteroduplex analysis (HET), chemical cleavage analysis (CCM), catalytic nucleic acid cleavage, or a combination thereof (see, for example, Lemieux, 2000; Langridge et al., 2001). The invention also includes the use of molecular marker techniques to detect allele-linked polymorphisms of (for example) the Sr26 gene that confers resistance to at least one strain of Puccinia graminis.These methods include the detection or analysis of restriction fragment length polymorphisms (RFLPs), RAPDs, amplified fragment length polymorphisms (AFLPs), and microsatellite polymorphisms (simple sequence repeats, SSRs). Closely linked markers can be readily obtained using well-established techniques such as bulk segregant analysis, reviewed by Langridge et al. (2001). In one embodiment, a loci linked for marker-assisted selection is at least within 1 cM, or 0.5 cM, or 0.1 cM, or 0.01 cM of a gene encoding a polypeptide of the invention. The polymerase chain reaction (POR) is a reaction in which replicate copies of a target polynucleotide are made using a primer pair or primer set consisting of an up-direction primer and a down-direction primer, and a polymerization catalyst, such as a DNA polymerase, and typically a thermally stable polymerase enzyme. Methods for PCR are well-known in the field and are taught, for example, in POR (MJ McPherson and SG Moller (editors), BIOS Scientific Publishers Ltd, Oxford, (2000)). PCR can be performed on cDNA obtained from reverse-transcribed mRNA isolated from plant cells expressing the Sr26 gene or allele, which confers resistance to at least one strain of Puccinia graminis. However, it is generally easier to perform PCR on genomic DNA isolated from a plant. A primer is an oligonucleotide sequence that can hybridize in a sequence-specific manner with the target sequence and be extended during PCR. Amplicons, PCR products, PCR fragments, or amplification products are extension products comprising the primer and newly synthesized copies of the target sequences. QAfrQQn / 1 znz / q / YILI Multiplex PCR systems contain multiple sets of primers, resulting in the simultaneous production of more than one amplicon. Primers may perfectly match the target sequence or may contain mismatched internal bases that can lead to the introduction of a restriction enzyme or catalytic nucleic acid recognition / cleavage sites into specific target sequences. Primers may also contain additional sequences and / or modified or labeled nucleotides to facilitate amplicon capture or detection. Repeated cycles of thermal DNA denaturation, primer hybridization to their complementary sequences, and extension of the hybridized primers with the polymerase result in exponential amplification of the target sequence. The terms target, target sequence, or template refer to the nucleic acid sequences that are amplified. Methods for direct sequencing of nucleotide sequences are well known to experts in the field and can be found, for example, in Ausubel et al. (supra) and Sambrook et al. (supra). Sequencing can be carried out using any suitable method, such as dideoxy sequencing, chemical sequencing, or variations thereof. Direct sequencing has the advantage of determining the variation in any base pair of a particular sequence. TILLING The plants of the invention can be produced using a process known as TILLING (Directing Locally Induced Lesions in Genomes). In the first stage, introduced mutations, such as novel single-base-pair changes, are induced in a plant population by treating seeds (or pollen) with a chemical mutagen. The plants are then advanced to a generation where the mutations are stably inherited. DNA is extracted, and seeds from all members of the population are stored to create a resource that can be accessed repeatedly over time. For a TILLING assay, PCR primers are designed to specifically amplify a single target gene of interest. Specificity is especially important if a target is a member of a gene family or part of a polyploid genome. Dye-labeled primers can then be used to amplify PCR products from pooled DNA from multiple individuals. These PCR products are denatured and re-hybridized to allow the formation of unpaired base pairs. Unpaired bases, or heteroduplexes, represent both naturally occurring single nucleotide polymorphisms (SNPs) (i.e., many plants in the population are likely to have the same polymorphism) and induced SNPs (i.e., only rare individual plants are likely to have the same polymorphism). QAfrQQn / 1 znz / q / YILI show the mutation). After heteroduplex formation, the use of an endonuclease, such as Cel I, that recognizes and cleaves unpaired DNA is key to discovering new SNPs within a TILLING population. Using this approach, many thousands of plants can be screened to identify any individual with a single base change, as well as small insertions or deletions (1–30 bp) in any specific gene or region of the genome. The genomic fragments analyzed can range in size from 0.3 to 1.6 kb. With 8-fold pooling, 1.4 kb fragments (discounting the ends of fragments where SNP detection is problematic due to noise), and 96 lanes per assay, this combination allows for the screening of up to one million base pairs of genomic DNA per single assay, making TILLING a high-throughput technique. Tilling is described in more detail in Slade and Knauf (2005), and Henikoff et al. (2004). In addition to enabling the efficient detection of mutations, high-throughput TILLING technology is ideal for detecting natural polymorphisms. Therefore, interrogating an unknown homologous DNA sequence using heteroduplexes against a known sequence reveals the number and position of polymorphic sites. Both nucleotide changes and small insertions and deletions are identified, including at least some repeat-number polymorphisms. This process has been termed Ecotilling (Comal et al., 2004). Each SNP is recorded by its approximate position within a few nucleotides. Therefore, each haplotype can be archived based on its mobility. Sequence data can be obtained with relatively small incremental effort using aliquots of the same amplified DNA used for the unpaired excision assay. The left or right sequencing primer for a single reaction is chosen by its proximity to the polymorphism. The Sequencher software performs multiple alignment and detects the base change, which in each case confirms the gel band. Ecotilling can be performed more economically than whole-scale sequencing, the method currently used for most SNP discoveries. Plates containing ecotypic DNA in matrix can be screened instead of DNA clusters from mutagenized plants. Because detection is performed on gels with near base-pair resolution and the background patterns are uniform across the lanes, bands of identical size can be paired, discovering and genotyping SNPs in a single step. This makes final SNP sequencing simple and efficient, further enhanced by the fact that aliquots of the same PCR products used for screening can be subjected to DNA sequencing. Plant / Qrano Processing The grains / seeds of the invention, preferably cereal grain and more preferably wheat grain, or other plant parts of the invention, can be processed to produce a food ingredient, food product or non-food product using any technique known in the art. In one form, the product is whole grain flour, such as ultrafinely milled whole grain flour, or flour made from approximately 100% of the grain. Whole grain flour includes a refined flour component (refined flour) and a coarse fraction (an ultrafinely milled coarse fraction). Refined flour can be flour that is prepared, for example, by milling and sifting clean grains, such as wheat or barley. The particle size of refined flour is described as flour in which at least 98% passes through a screen with openings no larger than those of woven wire mesh called 212 micrometers (US 70 mesh). The coarse fraction includes at least one of the following: bran and germ. For example, the germ is an embryonic plant found within the kernel of the grain. The germ contains lipids, fiber, vitamins, proteins, minerals, and phytonutrients, such as flavonoids. The bran consists of several layers of cells and has a significant amount of lipids, fiber, vitamins, proteins, minerals, and phytonutrients, such as flavonoids. Additionally, the coarse fraction may include an aleurone layer, which also contains lipids, fiber, vitamins, proteins, minerals, and phytonutrients, such as flavonoids.The aleurone layer, although technically considered part of the endosperm, exhibits many of the same characteristics as the bran and is therefore normally removed along with the bran and germ during the milling process. The aleurone layer contains proteins, vitamins, and phytonutrients, such as ferulic acid. Furthermore, the coarse fraction can be blended with the refined flour constituent to form wholemeal flour, thus providing a wholemeal flour with higher nutritional value, fiber content, and antioxidant capacity compared to refined flour. For example, the coarse fraction or wholemeal flour can be used in varying quantities to replace refined or wholemeal flour in baked goods, snack products, and food products. The wholemeal flour of the present invention (i.e., ultrafinely milled wholemeal flour) can also be marketed directly to consumers for use in their homemade baked goods. In one exemplary embodiment, the granulation profile of the wholemeal flour is such that 98% of the particles by weight of the wholemeal flour are smaller than 212 micrometers. In additional methods, the enzymes found within the bran and germ of wholemeal flour and / or the coarse fraction are inactivated to stabilize the wholemeal flour and / or coarse fraction. Stabilization is a process that uses steam, heat, radiation, or other treatments to QAfrQQn / L7n7 / 3 / YILI inactivates the enzymes found in the bran and germ layer. The stabilized flour retains its cooking characteristics and has a longer shelf life. In additional forms, wholemeal flour, coarse fraction or refined flour may be a component (ingredient) of a food product and may be used to produce a food product. For example, the food product could be a bagel, a cookie, a loaf, a bun, a croissant, a dumpling, an English muffin, a muffin, a pita bread, a quick bread, a refrigerated / frozen dough product, dough, baked beans, a burrito, chili, a taco, a tamale, a tortilla, a cake, a ready-to-eat cereal, a ready-to-eat meal, filling, a microwave meal, a brownie, a pie, a cheesecake, a coffee cake, a biscuit, a dessert, a pastry, a sweet roll, a chocolate bar, a pie crust, pie filling, baby food, a baking mix, a batter, a breading, a sauce mix, a meat thinner, a meat substitute, a seasoning mix, a soup mix, a gravy, a roux,a salad dressing, a soup, sour cream, a noodle, a pasta, ramen noodles, chow mein noodles, lo mein noodles, an ice cream inclusion, an ice cream bar, an ice cream cone, an ice cream sandwich, a cracker, a crouton, a donut, an egg roll, an extruded snack, a fruit and grain bar, a microwaveable snack product, a nutrition bar, a pancake, a par-baked bakery product, a pretzel, a pudding, a granola-based product, a snack chip, a snack, a snack mix, a waffle, a pizza base, animal food or pet food. In alternative embodiments, wholemeal flour, refined flour, or coarse flour may be a component of a nutritional supplement. For example, the nutritional supplement may be a product added to the diet that contains one or more additional ingredients, which generally include vitamins, minerals, herbs, amino acids, enzymes, antioxidants, spices, probiotics, extracts, prebiotics, and fiber. The wholemeal flour, refined flour, or coarse flour of the present invention includes vitamins, minerals, amino acids, enzymes, and fiber. For example, the coarse flour contains a concentrated amount of dietary fiber, as well as other essential nutrients, such as B vitamins, selenium, chromium, manganese, magnesium, and antioxidants, which are essential for a healthy diet. For example, 22 grams of the coarse flour of the present invention provides 33% of an individual's recommended daily fiber intake.A nutritional supplement may include any known nutritional ingredient that contributes to an individual's overall health. Examples include, but are not limited to, vitamins, minerals, other fiber components, fatty acids, antioxidants, amino acids, peptides, proteins, lutein, ribose, omega-3 fatty acids, and / or other nutritional ingredients. The supplement may be provided in the following forms, among others: instant drink mixes, ready-to-drink beverages, nutrition bars, wafers, cookies, crackers, and gel injections. QRbQQn / 1707 / 3 / YILI capsules, chewable tablets, chewable tablets, and pills. One formulation provides the fiber supplement in the form of a flavored shake or malt-type beverage; this formulation may be particularly attractive as a fiber supplement for children. In a further embodiment, a milling process can be used to make a multigrain flour or a multigrain coarse fraction. For example, the bran and germ of one type of grain can be milled and blended with milled endosperm or whole grain flour from another type of grain. Alternatively, the bran and germ of one type of grain can be milled and blended with milled endosperm or whole grain flour from another type of grain. The present invention is contemplated to encompass blending any combination of one or more of the bran, germ, endosperm, and whole grain flour from one or more grains. This multigrain approach can be used to make customized flour and capitalize on the qualities and nutritional content of multiple types of cereal grains to produce a single flour. It is envisaged that the wholemeal flour, coarse fraction, and / or grain products of the present invention may be produced by any milling process known in the art. One exemplary embodiment involves milling the grain in a single stream without separating the endosperm, bran, and germ into separate streams. The clean, tempered grain is conveyed to a primary mill, such as a hammer mill, roller mill, spike mill, impact mill, disc mill, air-wear mill, hole mill, or similar. After milling, the grain is discharged and conveyed to a sieve. Furthermore, it is envisaged that the wholemeal flour, coarse fraction, and / or grain products of the present invention may be modified or improved by numerous other processes, such as fermentation, instantizing, extrusion, encapsulation, roasting, or similar methods. Malted A malt-based beverage provided by the present invention includes alcoholic beverages (including distilled beverages) and non-alcoholic beverages produced using malt as part or all of their starting material. Examples include beer, happoshu (a low-malt beer beverage), whiskey, low-alcohol malt-based beverages (e.g., malt-based beverages containing less than 1% alcohol), and non-alcoholic beverages. Malting is a process of controlled soaking and germination followed by drying of grains such as barley and wheat. This sequence of events is important for the synthesis of numerous enzymes that cause grain modification, a process that primarily depolymerizes the cell walls of the dead endosperm and mobilizes the grain's nutrients. In the subsequent drying process, flavor and color are produced due to chemical reactions. QAfrQQn / 1 znz / q / YILI pardeamlento. Although the main use of malt is for the production of beverages, it can also be used in other industrial processes, for example, as a source of enzymes in the baking industry, or as a flavoring and coloring agent in the food industry, for example as malt or as a malt flour, or indirectly as a malt syrup, etc. In one embodiment, the present invention relates to methods for producing a malt composition. The method preferably comprises the steps of: (i) providing grain, such as barley or wheat, of the invention, (ii) soaking said grain, (iii) germinating the soaked grains under predetermined conditions and (iv) drying said germinated grains. For example, malt can be produced by any of the methods described in Hoseney (Principles of Cereal Science and Technology, Second Edition, 1994: American Association of Cereal Chemists, St. Paul, Minnesota). However, any other suitable method for producing malt, such as methods for producing specialty malts, including but not limited to methods for roasting malt, may also be used with the present invention. Malt is primarily used for brewing beer, but also for producing distilled spirits. The brewing process includes wort production, primary and secondary fermentations, and post-treatment. First, the malt is milled, stirred with water, and heated. During this mashing process, enzymes activated during malting break down the grain's starch into fermentable sugars. The resulting wort is then clarified, yeast is added, the mixture is fermented, and post-treatment is performed. EXAMPLES EXAMPLE 1 - MATERIALS AND METHODS MutRenSeq Set Plant materials and preparation of mutated DNA Avocet + Lr46 line seeds (Avocet carries Sr26) were treated with ethyl methanesulfonate (EMS) following the protocol described by Mago et al. (2005). Initially, a mortality curve was generated in 20 grains at different concentrations: 0.2, 0.4, 0.6, 0.7, and 1.0% (v / v) to identify the dose required to achieve 50% mortality. M2 families obtained as offspring from one ear of each M1 plant were analyzed to determine their response to stem rust. Individual plants from the segregating offspring were cultured, and the progeny were analyzed. From these offspring, susceptible and resistant homozygous sibling pairs were recovered. QAfrQQn / I 7Π7 / 3 / YΙΛΙ Genomic DNA was isolated from healthy leaves of selected seedlings following the protocol described by Yu et al. (2017). DNA quality and quantity were first verified using a NanoDrop spectrophotometer (Thermo Scientific) and then with a 0.8% agarose gel. Enrichment and sequencing of resistance genes (RenSeq) NLR Target enrichment was performed by Arbor Biosciences (Ann Arbor, USA) following the MYbaits protocol using an enhanced version of the previously published Triticeae bait library available at github.com / steuernb / MutantHunter. Library construction was performed following the TruSeq RNA v2 protocol. All enriched libraries were sequenced on a HiSeq 2500 (Illumina) using 250 bp paired end reads and SBS chemistry. MutantHunter To identify Sr26 contig from mutants, the inventors followed the MutantHunter ensemble with all the default parameters of Steuernage et al. (2016), except for the use of CLC Genomics Workbench (V9) for quality control reads, trimming, de novo assembly of wild-type Avocet, and mapping of all reads against the de novo wild-type assembly. Mutants M1 and M5 were likely siblings because they shared the same mutated SNP. Obtaining full-length genes, confirming candidate contigs, and confirming genetic structure Total RNA was extracted using the PureLink™ RNA Mini Kit (Invitrogen) according to the manufacturer's instructions. cDNA synthesis was performed using the method described by the manufacturer (Clontech). The full gene length was amplified using the 5' and 3' RACE (Rapid cDNA End Amplification) kit (Clontech). The 5' and 3' untranslated regions (UTRs) were obtained using a genomic targeting kit (Clontech). All mutants used in the RenSeq array were reconfirmed by Sanger sequencing, and each unique SNP in the four mutants resulted in either an amino acid substitution or a splice. Predicted exon-intron structures were confirmed by full cDNA amplification and RNA sequencing data. Transchemical validation The Sr26 gene was introduced into the Fielder wheat crop via the pVecBARII binary vector using the Agrobacterium transformation protocol described by Ishida et al. (2015) and QRbQQn / I7P7 / 3 / YILI phosphinothricin as a selective agent. T0 shoots were transplanted from petridish to a growth cabinet with a daytime and nighttime temperature of 23 °C, 16 hours of light and 8 hours of darkness. The plants were inoculated with Pgt races 7-10 days after transplanting and scored at 10-15 days as described by McIntosh (1995). Phenotyping under greenhouse and field conditions Phenotyping of stem rust responses in seedlings and adult plants in the greenhouse or in the field was carried out according to the methods described by Bender et al. (2016) and Pretorius et al. (2015). Chitin assay and histological evaluation The chitin assay was performed according to the protocol described by Ayliffe (2013). All results were based on three biological and technical replicates. For the histological evaluation, measurements of the average size of individual colonies were performed according to the protocol described by Ayliffe (2013), except that the plant tissue was not weighed during sampling. After adding KOH, the tubes containing plant tissue were incubated at 60 °C overnight before being washed three times with 50 µL Tris (pH 7.0). Three to six ml of 50 µL Tris were added to the samples after washing. A 1 mg / ml solution of FITC probe (Sigma-Aldrich) of wheat germ agglutinin (WGA) diluted in water was added to a concentration of 7 µL / ml and allowed to stain for 1.5 h. Individual colonies in each sample were measured using a WU epifluorescence cube (450–480 nm excitation filter and 515 nm barrier filter) on an Olympus AX70 microscope (Tokyo, Japan). The length and width of the fluorescent colonies were measured to approximate the colony size (pm2). Microscopic images were captured using a CC12 digital camera and AnalySIS LS Research software version 2.2 (Olympus Soft Imaging System, Japan). The average size was calculated for 15–20 infection sites per sample, each replicated in three independent treatments. Phylogenetic tree construction The R gene protein sequences found in the NCBI database were aligned using T-Coffee and the phylogenetic tree generated using Mega7. CC domain prediction and CC conserved domain alignment The coiled coil domains were determined using the COILS prediction program (Lupas et al., 1991) (https: / / embnet.vital-it.ch / software / COILS_form.html). QAfrQQn / 1 znz / q / YILI T-Coffee Expresso (http: / / tcoffee.crg.cat / apps / tcoffee / do:expresso) was used for protein sequence alignment. Plant growth conditions and transient expression analysis N. benthamiana plants were grown in a growth chamber at 23 °C with a light period of 16 h. For transient expression analyses in N. benthamiana, pBIN19-derived vector constructs were transformed into the Agrobacterium tumefaciens strain GV3101_pMP90, and pAM-PAT vector constructs were transformed into GV3103. Bacterial strains were grown in Luria-Bertani liquid medium containing 50 mg / mL rifampicin, 15 mg / mL gentamicin, and 25 mg / mL kanamycin (and 25 mg / mL carbenicillin for pAM-PAT vectors) at 28 °C for 24 h. The bacteria were collected by centrifugation, resuspended in infiltration medium [10 mM MES (pH 5.6), 10 mM MgCl2, and 150 pM acetosyringone] at an OD600 in the range of 0.5 to 1, and incubated for 2 h at room temperature before leaf infiltration. For each independent infiltration experiment, each construct was infiltrated onto three leaves from three or four individual plants.The infiltrated plants were incubated in growth chambers under controlled conditions for all subsequent trials. To document cell death, the leaves were photographed 2–5 days after infiltration. Construct generation, protein excretion, and immunotransfer The CC domains of the Sr polypeptides were aligned to the first 160 amino acids of the Sr33 polypeptide sequence. The selected CC domain was fused with its native C-terminus stop codon by PCR and cloned into a pDonor vector. Subsequently, it was transferred into pB1N19 target vectors with cloning gateway N-terminus YFP fusions (Invitrogen®). Sequences were verified after each transformation. Protein extraction from N. benthamiana leaves was performed as described by Cesari et al. (2013). For immunoblotting analysis, proteins were separated by SDS-PAGE and transferred to a nitrocellulose membrane (Pall). The membranes were blocked in 5% skim milk and probed with anti-HA (Roche anti-HA 12CA5 or Roche anti-HA-HRP 3F10) and anti-GFP (Roche). The labeling was detected using the SuperSignal West Femto (Pierce) chemiluminescence kit.The membranes were stained with Ponceau S to confirm equal charge. Specific gene marker A panel of wheat gene pools postulated to possess Sr26 was used to validate gene-specific primers. A primer set designed to flank the junction of intron I and exon II, with an amplicon size of 1,580 bp, was confirmed to be QAfrQQn / L7n7 / 3 / ΥΙΛΙ highly specific for the target gene (Sr26GSPF; 5'-GGAATACTCGAATACCAGGCCAT-3' (SEQ ID NO:30); Sr26GSPR; 5'-TTGCCACTGTGAACATGTTTATAGAT-3' (SEQ ID NO:31)). EXAMPLE 2 - CLONING Sr26 The inventors identified susceptible mutants derived from ethyl methanesulfonate (EMS) from the background Avocet+Lr46. Five independent mutants (four with presumed point mutations and one with a presumed deletion) together with wild-type Avocet+Lr46 were used in a RenSeq pool (Figure 1a and Figure 2a). A single 2,470 bp contig was identified using MutantHunter (Steuernage et al., 2016) (Figure 2b). The complete Sr26 sequence is 6,066 bp and consists of two exons and a 3,258 bp intron. The encoded 935-amino-acid protein contains a coiled (CC) domain at the N-terminus, followed by the NB-ARC domain and then the LRR motifs at the C-terminus (Figure 1b). The seven cloned wheat stem rust race-specific R protein sequences Sr13, Sr21, Sr22, Sr33, Sr35, Sr45, and Sr50 were aligned with Sr26 and its homologs on CSrefvl .0 chromosomes 6A, 6B, and 6D by Expresso using structural information. The CC, NB-ARC, LRR domains and conserved motifs were aligned as shown in Figure 3. All amino acid changes caused by the EMS mutation of Sr26 were localized to conserved motifs within the NB-ARC domain. The 128S1 mutant has an alanine-to-threonine change within the RNBS-C motif, while the 70S1 mutant (and the 12S1 mutant) has a serine-to-asparagine change in the RNBS-D motif. The 499S1 mutant has an alternative splicing form that resulted in a deletion of 22 amino acids in the RNBS-D motif (Figure 3). EXAMPLE 3 - TRANSGENIC VALIDATION OF Sr26 A complementary transgenic experiment was conducted to clarify whether the candidate gene Sr26 was responsible for resistance in wheat. Because the initially obtained 5' and 3' UTRs were less than 1 kb (917 bp and 263 bp, respectively), there was a potential risk of insufficient regulatory elements that could impair proper gene expression. To ensure expression of the candidate gene, three constructs were used to produce transgenic wheat (Figure 4a). One construct was assembled with the obtained native 5' and 3' UTRs and designated Fielder:Sr26:NativeRE (Regulatory Elements). The other two constructs, designated Fielder:Sr26:Sr22RE and Fielder:Sr26:Sr33RE, were fused with the obtained native 5' and 3' UTRs along with the regulatory elements from either Sr22 or Sr33 genes. Twenty-one, 22 and 14 independent primary transgenic lines carrying Fielder:Sr26:NativeRE, Fielder:Sr26:Sr22RE and Fielder:Sr26:Sr33RE, respectively. QAfrQQn / L7n7 / 3 / YILI All independent primary transgenic T0 plants of Fielder:Sr26:NativeRE, Fielder:Sr26:Sr22RE, and Fielder:Sr26:Sr33RE showed resistance to stem rust pathotype 98-1,2,3,5,6, while all empty vector transformed Fielder controls were susceptible (Figure 4b, Table 2). To test the responses of Sr26 to rust against newly emerged Pgt pathotypes, the Pgt races PTKST (collected in South Africa), TTRTF (collected in Italy and Eritrea), TKKTF (collected in Italy), and PCHSF (collected in Georgia) were used for phenotyping. In all cases, wild-type Sr26 showed resistance, while the Sr26 mules were susceptible to each pathotype (Table 2). EXAMPLE 4: EXPLORATION OF Sr26 HOMOLOGUES IN GRASS, DIPLOID WHEAT, AND OTHER PLANT GENOMES According to BLAST best hits against IWGSC CS ref v1.0, the location of the closest homologs of candidate Sr26 in the Chinese Spring v1.0 reference is consistent with previous studies showing that this gene occurs on the homologous chromosome group six. The inventors further extended the BLAST interval of Sr26 to diploid wheat and grass genomes, including T. monococcum, Aegilops tauschii, Ae. speltoides, Ae. sharoneenesis, and T. urartu (Figure 5). EXAMPLE 5 - STRUCTURAL ANALYSIS OF PLANT CNL-TYPE IMMUNE RECEPTOR PROTEIN To determine the evolutionary distance and degree of diversity between Sr26 and other cloned plant CNL-type R genes at the protein sequence level, the inventors selected 124 CNL-type R genes and performed a phylogenetic analysis (Figure 6). The R gene closest to Sr26 in the selected group is the wheat stem rust resistance gene Sr13. The largest subgroup of wheat rust R genes includes Sr33, Sr50, Sr35, and Sr22, which are clustered with the MLA R gene family. The wheat stem rust gene Sr45 is clustered with the wheat powdery mildew R gene Pm3 and is far removed from other wheat rust R genes. The wheat stem rust gene Sr21 was closest to Pm2, Lr21, and the wheat nematode R genes Crei and Cre3. QRbQQn / 1 znz / q / YILI Table 2: Phenotypic response score of Sr26 against various Pgt pathotypes. a. Stem rust scores of six entries under greenhouse and field conditions, at both seedling and adult plant stages, when inoculated with PTKST. Equivalent results were obtained in three independent experiments. b. Rust test result of Sr26 against various Pgt pathotypes. QAfrQQn / L7n7 / 3 / YILI Entries Adult Plant Stage Leaf Infection Rate Field Score Stem Severity Stem Infection Type Leaf Infection Type Avocet-Li I6 20MR 12- :l- 50MRMS Axocet-Li? I-Li I6-L167 20RMR .1 .1 30RMR Kire (Sr261 20MR 12- : 1 2C :l- 40MR Si26mutant(!2SI vOMSS > — 1 oos Si26 mutant(499S) 30MSS > ; Ϊ · 1 oos Line 37 ?0MSS s — idos Paioiipo ​​pgt TTRTF TKKTF PCHSF PTKST Srlo Wild type 1 1- 1- Mutant 3- 2 — EXAMPLE 6 - CELL DEATH INDUCTION TESTS FOR DOMAINS Sr50, Sr33, Sr35, Sr22, Sr45, Sr46 AND Sr26 CC The CC domains of some R-type CNL genes, including Sr33 and Sr50, have been shown to trigger cell death in N. benthamiana. To test this function more generally for wheat CNL, constructs expressing CC domains of Sr26, Sr22, Sr35, Sr45, and Sr46 were generated for transient expression assays and compared with constructs expressing CC domains of Sr50 and Sr33 as controls. To define the minimum length of the CC domains to be tested, the protein sequences of the seven genes were aligned with Sr33 and Sr50. The CC domain of all genes was truncated at the corresponding 160aa site of Sr33, which has previously been shown to be sufficient for CC domain induction of cell death.It has been previously reported that secondary structures have an effect on protein stability; therefore, the sequences were appropriately trimmed to maintain the protein's secondary structure units intact when determining the CC domain boundary. The predicted secondary structures of each protein's CC domain were generated using PSIPRED v3.3 software via the PSIPRED server (http: / / bioinf.cs.ucl.ac.uk / psipred / ) (Figure 7a). Secondary structure predictions using PSIPRED v3.3 suggest that all these CC domain fragments include the four helices of the known CC domain structure. It was demonstrated that, in addition to Sr33 and Sr50, the CC domains of Sr35 and Sr46 are also sufficient for inducing cell death in plants. The CC domain of two novel wheat stem rust resistance genes, Sr35 and Sr46, is sufficient to trigger cell death in plants when fused with the N-terminus YFP marker (Figure 7b). In contrast, no cell death was observed when the CC domain protein of Sr26, Sr45, and Sr22 in A. benthamiana was expressed fused with the same marker (Figure 7b). However, Western blot analyses (Figure 7c) showed no detectable protein for Sr22 CC and low levels of CC domains for Sr26 and Sr45, which may explain the lack of cell death induction (Figure 7c). In some cases, marker fusion can interfere with protein expression and function. To avoid the potentially negative effect of the marker, the inventors tested the function of the CC domains of Sr22, Sr26, and Sr45 without the marker. Interestingly, the CC domain of Sr22 was able to trigger cell death in N. benthamiana plants without the fused marker. However, in the case of the CC domains of Sr26 and Sr45, without the marker, no cell death induction was observed (Figure 8). EXAMPLE 7 - ENHANCING Sr26 RESISTANCE IN COMBINATION WITH APR GENES To improve the deployment of Sr26 to achieve long-lasting resistance, materials incorporating three pleiotropic genes Lr34 / Yr18 / Sr57, Lr46 / Yr29 / Sr58, and Lr67 / Yr46 / Sr56 were generated on an Avocet S background. The stem rust response of Kite (Sr26), Avocet (Sr26)+Lr46, Avocet (Sr26)+Lr34+Lr46+Lr67, along with the Sr26 12S and 499S mutants, were compared at the seedling and adult plant stages under greenhouse and field conditions. Greenhouse experiments included phenotyping on seedling leaves (Figure 9a, 9b; Table 2), adult plant stems (Figure 9c, 9d; Table 2), adult plant flag leaves and leaf sheaths (Figure 10a, 10b), while adult plant stems were rated in the field. A chitin assay was also performed on flag leaf sheaths from adult plants (Figure 10c), and the average individual PTKST colony size was measured at 4 dpi (Figure 10c). QAfrQQn / 1 znz / q / YILI 10d). In all cases, Avocet (Sr26)+Lr34+Lr46+Lr67 showed stronger resistance compared to Kite (sr26) and Avocet (Sr26)+Lr46. No additive or synergistic effect has been previously reported among the three APR genes Lr34, Lr46, and Lr67, but additive resistance has been found when Lr34 or Sr26 is combined with other genes. Since the type of infection produced by Avocet (Sr26) + Lr46 was not as strong as the resistance conferred by the three APRs involved in the line containing Sr26, this suggests that such synergism is unlikely due to the interaction between Lr46 and Sr26. To test these Fielder lines containing each APR gene alone, each individual APR with Sr26, two APR genes alone, two APR genes combined with Sr26, and three APR genes alone from a non-infectious population (NIL) at the seedling and adult plant stages, lines could be generated and grown. The resulting plants could then be infected with Puccinia graminis, and the type of infection classified as described. EXAMPLE 8 - ANALYSIS Eight stem rust resistance genes have been cloned at all stages, originating from *T. monococcum* (Sr21, Sr22, and Sr35), the A genome donor of hexaploid bread wheat; *Ae. tauschii* (SR33 and SR45), the D genome donor of hexaploid bread wheat; diploid rye (Sr50); and durum wheat (Sr13). Sr26 is the first wheat stem rust R gene identified in tall wheatgrass (*T. ponticum*). Furthermore, Sr26 and Sr50 are the only two Sr genes in the bread wheat tertiary gene pool. The present invention relates to Sr26, a locus with the broadest resistance to *Pgt* isolates worldwide; it is a unique gene encoding a CNL-type immune receptor protein. The inventors also demonstrated that the Sr26 coding region, along with its minimal native UTR regions (917 bp at the 5' and 263 bp at the 3' positions, respectively), was sufficient to confer resistance. The addition of Sr22 and Sr33 regulatory elements fused with native Sr26 promoter and terminator assemblies was tested in T0 plants. All T0 plants carrying the chimeric Sr26 gene fusions exhibited a resistance phenotype when tested with the Pgt 98-1,2,3,5,6 race. Hatta et al. (2018) reported that Sr45 gene function is not compromised when driven by Sr33 regulatory elements. Here, the Sr22 and Sr33 promoter and terminator were found not to negatively affect Sr26 gene expression. The conserved motifs of the NB-ARC domain are among the most conserved residues in R proteins, suggesting an important functional and structural role. This is found to be true for Sr26 based on the mutated position of all Sr26 mutants (the 128S mutant is in RNBS-B, 70S / 12S and 499S1 are in RNBS-D), and for Sr50 (M13 mutant in RNBS-B) and Sr33 (E9 and E7 mutants in the p-loop, E6 in RNBS-B, and E8 in GLPL). The importance of these domains in CNL gene function is further emphasized. QAfrQQn / 1 znz / q / YILI The nucleotide-binding leucine-rich repeat receptor (NLR) has long been recognized as an immune receptor in plants. TIR-containing (TNL) NLRs and CC-containing (CNL) NLRs are two main classes of plant NLRs, defined by the presence of a TIR or CC domain at their N-terminus. Most, if not all, NLRs in cereals belong to the CNL class. Although both TIR and CC domains have been considered predominant signaling elements of NLRs, they differ significantly from each other structurally and functionally (Ve et al., 2015). In contrast to intensive studies of the TIR domain, the structure and function of CC domain signaling, specifically how it directs effector perception, remain largely unknown. Previous studies have revealed diverse functions of CC domains, including their ability to self-associate, induce cell death, and interact with other proteins as cofactors.For example, the EDVID motif of the CC domain has been reported to play a role in regulating the interaction with the NB domain of Rx (Hao et al., 2013). The CC domains of MLA10 and RPM1 also have the conserved EDVID motif, but only the CC domain of MLA10 is capable of signaling cell death, whereas the CC domains of MLA10 and RPM1, but not Rx, can self-associate. The CC domains of RPM1 and Rx interact with cofactors required for pathogen clearance, while no such interactions are known for MLA10. Maekawa et al. (2011) and Cesari et al. (2013) reported that the CC domains MLA10, Sr33, and Sr50 can induce cell death in N. benthamiana. The present inventors have found that the CC domains of Sr35, Sr46, and Sr22, expressed without a marker, induced cell death in the plant. However, the CC domains of Sr26 and Sr45 did not induce cell death in the plant. In the case of the CC domain RX, no induced cell death was observed in the model host plant, even though the construct used included it. These results suggest that the induction of cell death by CC domains appears to be a common feature in stem rust resistance genes, and further studies are needed to further elucidate the reason behind this divergence in cell death induction by the CC domain of the R gene. Those skilled in the art will appreciate that numerous variations and / or modifications can be made to the invention as shown in the specific embodiments without departing from the spirit or scope of the invention as broadly described. Therefore, the present embodiments should be regarded in all respects as illustrative and not restrictive. This application claims priority of AU 2018904568 filed on November 30, 2018, the full content of which is incorporated herein by reference. All publications analyzed and / or referenced herein are incorporated herein in their entirety. QAfrQQn / Lznz / q / YILI Any analysis of documents, acts, materials, devices, articles, or the like included in this specification is solely for the purpose of providing context for the present invention. It should not be taken as an admission that any or all of these matters form part of the basis of the prior art or were common knowledge in the field relevant to the present invention as it existed prior to the priority date of each claim in this application. This invention was made with government support pursuant to grant (965429) from the National Science Foundation. The government has certain rights in and to this invention. QAfrQQn / L7n7 / 3 / YILI REFERENCES Abdullah et al. (1986) Biotechnology 4:1087. Ayliffe et al. (2011) Mol Plant Microbe. Interact. 24:1143-1155. Bam et al. (2008) Proc S Afr Sug Technol Ass 81:508-512. Barker et al. (1983) Plant Mol. BioL 2:235-350. Begemann et al. (2017) SciRep. 7(1):11606. Bender et al. (2016) Plant Disease 100, 1627-1633. Bevan et al. (1983) Nuci. Acid Res. 11:369-385. Bhattacharya, S. (2017) Nature 542, 145. Bulgarelli et al. (2010) PLoS One 5:e12599. Cadwell y Joyce (1992) PCR Methods Appl. 2:28-33. Capecchi (1980) Cell 22:479-488. 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Claims

1. A plant comprising an exogenous polynucleotide encoding a polypeptide conferring resistance to at least one strain of Puccinia graminis, wherein the polypeptide comprises amino acids having a sequence as indicated in SEQ ID NO:1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO:

1.

2. The plant of claim 1, wherein the polynucleotide is operatively linked to a promoter capable of directing the expression of the polynucleotide in a cell of the plant.

3. The plant of claim 1 or claim 2, wherein Puccinia graminis is Puccinia graminis f. sp. tritici.

4. The plant according to any one of claims 1 to 3, wherein the strain is one or more or all of the TTRTF, PTKST, TKKTF, TKTTF and PCHSF races of Puccinia graminis f. sp. tritici.

5. The plant according to any one of claims 1 to 4 having improved resistance to at least one strain of Puccinia graminis compared to an isogenic plant lacking the exogenous polynucleotide.

6. The plant according to any one of claims 1 to 5, wherein the polynucleotide comprises nucleotides having a sequence as provided in SEQ ID NO:2, a sequence that is at least 70% identical to SEQ ID NO:2, or a sequence that is hybridized to SEQ ID NO:

2.

7. The plant according to any one of claims 1 to 6, wherein i) the polypeptide comprises amino acids having a sequence that is at least 90% identical to SEQ ID NO:1, and / or i) the polynucleotide comprises a sequence that is at least 90% identical to SEQ ID NO:

2.

8. The plant according to any one of claims 1 to 7, wherein the polypeptide comprises one, more or all of a coiled domain (CC), a nucleotide-binding domain (NB) and a leucine-rich repeat (LRR) domain.

9. The plant according to any one of claims 1 to 8, which is a cereal plant, such as a wheat plant.

10. The plant according to any one of claims 1 to 9 comprising one or more additional exogenous polynucleotides encoding another plant pathogen resistance polypeptide.

11. The plant according to any one of claims 1 to 10, which is homozygous for the exogenous polynucleotide QAfrQQn / 1 znz / q / YILI 12. The plant according to any one of claims 1 to 11 growing in a field.

13. A population of at least 100 plants according to any one of claims 1 to 12 growing in a field.

14. A process for identifying a polynucleotide encoding a polypeptide that confers resistance to at least one strain of Puccinia graminis comprising: i) obtaining a polynucleotide operationally linked to a promoter, wherein the polynucleotide encodes a polypeptide comprising amino acids having a sequence as provided in SEQ ID NO:1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO:1, ii) introducing the polynucleotide into a plant, ii) determining whether the level of resistance to Puccinia graminis is altered relative to an isogenic plant lacking the polynucleotide, and iv) optionally, selecting a polynucleotide that, when expressed, confers resistance to Puccinia graminis.

15. The process of claim 14, wherein one or more of the following are applied: a) the polynucleotide comprises nucleotides having a sequence as provided in SEQ ID NO:2, a sequence that is at least 82% identical to SEQ ID NO:2, or a sequence that hybridizes with SEQ ID NO:2; b) the plant is a cereal plant such as a wheat plant; c) the polypeptide is a plant polypeptide or a mutant thereof; and d) step i) further comprises stably integrating the operatively linked polynucleotide into a promoter in the plant genome.

16. The process of claim 14 or claim 15, wherein the strain is one or more or all of the race TTRTF, PTKST, TKKTF, TKTTF and PCHSF of Puccinia graminis f. sp. tritici.

17. A substantially purified and / or recombinant polypeptide conferring resistance to at least one strain of Puccinia graminis, wherein the polypeptide comprises amino acids having a sequence as provided in SEQ ID NO: 1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO:

1.

18. The polypeptide of claim 17 comprising amino acids having a sequence that is at least 80% identical, at least 90% identical, or at least 95% identical to SEQ ID NO:

1.

19. An isolated and / or exogenous polynucleotide comprising nucleotides having a sequence as provided in SEQ ID NO: 2, a sequence that is at least 70% identical to SEQ ID NO: 2, a sequence encoding a polypeptide of claim 17 or claim 18, or a sequence that hybridizes with SEQ ID NO:

2. QRbQQn / 1707 / 3 / YILI 20. A chimeric vector comprising the polynucleotide of claim 19.

21. The vector of claim 20, wherein the polynucleotide is operatively linked to a promoter.

22. A recombinant cell comprising an exogenous polynucleotide of claim 19, and / or a vector of claim 20 or claim 21.

23. The cell of claim 22, wherein the cell is a cereal plant cell, such as a wheat cell.

24. A method for producing the polypeptide of claim 17 or claim 18, wherein the method comprises expressing in a cell or cell-free expression system the polynucleotide of claim 19.

25. A non-human transgenic organism, such as a transgenic plant, comprising an exogenous polynucleotide of claim 19, a vector of claim 20 or claim 21 and / or a recombinant cell of claim 22 or claim 23.

26. A method for producing the cell of claim 22 or claim 23, wherein the method comprises the step of introducing the polynucleotide of claim 19, or a vector of claim 20 or claim 21, into a cell.

27. A method for producing a transgenic plant according to any one of claims 1 to 11, wherein the method comprises the steps of i) introducing a polynucleotide as defined in claim 19 and / or a vector of claim 21 into a plant cell, ii) regenerating a transgenic plant from the cell, and iii) optionally harvesting seeds from the plant, and / or iv) optionally producing one or more offspring plants from the transgenic plant, thereby producing the transgenic plant.

28. A method for producing a transgenic plant according to any one of claims 1 to 11, wherein the method comprises the steps of i) crossing two parent plants, wherein at least one plant is a transgenic plant according to any one of claims 1 to 11, ii) screening one or more offspring plants from the cross to detect the presence or absence of the polynucleotide, and iii) selecting an offspring plant comprising the polynucleotide, thereby producing the plant.

29. The method of claim 28, wherein at least one of the parent plants is a tetraploid or hexaploid wheat plant. QRbQQn / 1707 / 3 / YILI 30. The method of claim 28 or claim 29, wherein step i) comprises analyzing a sample comprising plant DNA for the polynucleotide.

31. The method according to any one of claims 28 to 30, wherein step i) comprises i) selecting offspring plants that are homozygous for the polynucleotide, and / or i) testing the plant or one or more offspring plants thereof to determine resistance to at least one strain of Puccinia graminis.

32. The method according to any one of claims 28 to 31, wherein the strain is one or more or all of the TTRTF, PTKST, TKKTF, and PCHSF races of Puccinia graminis f. sp. tritici.

33. The method according to any one of claims 28 to 32 further comprising (i) backcrossing the offspring of the cross of step (i) with plants of the same genotype as a first parental plant lacking a polynucleotide encoding a polypeptide conferring resistance to at least one strain of Puccinia graminis a sufficient number of times to produce a plant having most of the genotype of the first parent but comprising the polynucleotide, and (iv) selecting a descendant plant having resistance to at least one strain of Puccinia graminis.

34. The method according to any one of claims 27 to 33, wherein the method further comprises the step of analyzing the plant for at least one other genetic marker.

35. A plant produced using the method according to any one of claims 27 to 34.

36. The use of the polynucleotide of claim 19, or a vector of claim 20 or claim 21, to produce a recombinant cell and / or a transgenic plant.

37. The use of claim 36, wherein the transgenic plant has improved resistance to at least one strain of Puccinia graminis compared to an isogenic plant lacking the exogenous polynucleotide and / or vector.

38. A method for identifying a plant comprising a polynucleotide encoding a polypeptide conferring resistance to at least one strain of Puccinia graminis, wherein the method comprises the steps of i) obtaining a nucleic acid sample from a plant, and ii) screening the sample for the presence or absence of the polynucleotide, wherein the polynucleotide encodes a polypeptide of claim 17 or claim 18.

39. The method of claim 38, wherein the polynucleotide comprises nucleotides having a sequence as provided in SEQ ID NO:2, a sequence that is at least 70% identical to SEQ ID NO:2, or a sequence that hybridizes with SEQ ID NO:

2. QRbQQn / I7P7 / 3 / YILI 40. The method of claim 38 or claim 39 identifying a transgenic plant according to any one of claims 1 to 11.

41. The method according to any one of claims 38 to 40, further comprising producing a plant from a seed prior to step i).

42. A plant part of the plant according to any one of claims 1 to 11, 25 or 35.

43. The plant part of claim 42, which is a seed comprising an exogenous polynucleotide encoding a polypeptide conferring to at least one strain of Puccinia graminis.

44. A method for producing a plant part, wherein the method comprises, a) growing a plant according to any one of claims 1 to 11, 25 or 35, and b) harvesting the plant part.

45. A method for producing flour, wholemeal flour, starch or other product obtained from seeds, wherein the method comprises: a) obtaining the seed according to claim 43, and b) extracting the flour, wholemeal flour, starch or other product.

46. ​​A product made from a plant according to any one of claims 1 to 11, 25 or 35 and / or a plant part of claim 42 or claim 43.

47. The product of claim 46, wherein the part is a seed.

48. The product of claim 46 or claim 47, wherein the product is a food product or a drinking product.

49. The product of claim 48, wherein i) the food product is selected from the group consisting of: flour, starch, leavened or unleavened breads, pasta, noodles, animal fodder, animal feed, breakfast cereals, snacks, cakes, malt, beer, pastries and foods containing flour-based sauces, or i) the drinkable product is beer or malt.

50. The product of claim 46 or claim 47, wherein the product is not a food product.

51. A method for preparing a food product of claim 48 or claim 49, wherein the method comprises mixing seeds, or flour, wholemeal flour or seed starch, with another food ingredient.

52. A method for preparing malt, comprising the seed germination step of claim 43. QAfrQQn / I 7P7 / 3 / YILI 53. The use of a plant according to any one of claims 1 to 11, 25 or 35, or part thereof, as animal feed, or for producing animal feed or human feed.

54. A composition comprising one or more of a polypeptide of claim 17 or claim 18, a polynucleotide of claim 19, a vector of claim 20 or claim 21, or a recombinant cell of claim 22 or claim 23, and one or more acceptable carriers.

55. A method for identifying a compound that binds to a polypeptide comprising amino acids having a sequence as provided in SEQ ID NO: 1, a biologically active fragment thereof, or an amino acid sequence that is at least 70% identical to SEQ ID NO: 1, wherein the method comprises: i) contacting the polypeptide with a candidate compound, and i) determining whether the compound binds to the polypeptide.