ISOLATED DNA CONSTRUCT AND INSECTICIDAL COMPOSITION

Abstract

Compositions and methods for pest control are provided. The methods involve transforming organisms with one or more nucleic acid sequences encoding insecticidal proteins and one or more silencing elements. In particular, the nucleic acid sequences are useful for preparing plants and microorganisms with insecticidal activity. Therefore, transformed bacteria, plants, plant cells, plant tissues, and seeds are provided. The compositions consist of insecticidal nucleic acids and proteins from bacterial species. The sequences are used in constructing expression vectors for subsequent transformation in organisms of interest, including plants, and as probes for isolating other homologous (or partially homologous) genes.Molecular and culture stacks find use in the control, growth inhibition or extermination of pest populations of Lepidoptera, Coleoptera, Diptera, fungi, Hemiptera and nematodes and to produce compositions with insecticidal activity.

Description

ISOLATED DNA CONSTRUCT, STACKED CULTURE ENCODING PESTICIDE PROTEINS AND SILENCER ELEMENTS, AND COMPOSITION COMPRISING THEM REFERENCE TO THE LIST OF SEQUENCES PRESENTED ELECTRONICALLY A sequence listing named “6578_sequence_listing.txt”, created on Tuesday, January 26, 2016, and 587 kilobytes in size, is archived in a machine-readable format along with the description. The sequence listing is part of the description and is incorporated herein in its entirety for reference. CROSS-REFERENCE WITH RELATED PATENT APPLICATIONS This application claims priority over the provisional patent application of the U.S. US patent application no. 62 / 131564, filed on March 11, 2015 and US provisional patent application no. 62 / 287272, filed on January 26, 2016, incorporated in their entirety into this description by reference. FIELD This description pertains to the field of molecular biology. Stacks of PIP-72 polypeptide genes encoding pesticide proteins and silencing elements are provided. These proteins Pesticides, RNAi traits, and the nucleic acid sequences that encode them are useful for preparing pesticide formulations and in the production of transgenic plants resistant to pests. BACKGROUND OF THE INVENTION Biological control of agriculturally important insect pests using microbial agents, such as fungi, bacteria, or other insect species, offers an environmentally friendly and commercially attractive alternative to synthetic chemical pesticides. In general, the use of biopesticides presents a lower risk of contamination and environmental hazards, and they provide greater target specificity than traditional broad-spectrum chemical insecticides. Furthermore, biopesticides are often less expensive to produce, thus improving economic viability for a wide variety of crops. Certain species of microorganisms of the genus Bacillus are known to have pesticidal activity against a variety of insect pests, including Lepidoptera, Diptera, Coleoptera, Hemiptera, and others. Bacillus thuringiensis (Bt) and Bacillus popilliae are among the most successful biological control agents discovered to date. Pathogenicity to insects has also been attributed to strains of B. larvae, B. lentimorbus, B. sphaericus, and B. cereus. Microbial insecticides, particularly those Obtained from Bacillus strains, they have played an important role in agriculture as alternatives to chemical pest control. Crops with enhanced insect resistance have been developed by genetically engineering them to produce pesticidal proteins from Bacillus. For example, corn and cotton plants have been genetically engineered to produce pesticidal proteins isolated from Bt strains. These genetically engineered crops are now widely used in agriculture and have provided farmers with an environmentally friendly alternative to traditional insect control methods. While they have proven to be commercially very successful, these genetically modified, insect-resistant crops provide resistance only to a narrow range of economically important insect pests.In some cases, insects can develop resistance to different insecticidal compounds, which increases the need to identify alternative biological control agents for pest control. Consequently, new pesticide proteins with different ranges of insecticidal activity against insect pests are needed, e.g., insecticidal proteins that are active against a variety of insects of the order Lepidoptera and the order that include, but are not limited to, insect pests that have developed resistance to existing insecticides. SUMMARY Compositions and methods are provided for conferring pesticidal activity to bacteria, plants, plant cells, tissues, and seeds. The compositions include nucleic acid molecules encoding sequences for the pesticide and insecticidal polypeptide PIP-72 and polynucleotides encoding RNAi silencing elements, vectors comprising those nucleic acid molecules, and host cells comprising the vectors. The nucleic acid sequences can be used in DNA constructs or expression cassettes for transformation and expression in organisms, including microorganisms and plants. The nucleotide or amino acid sequences can be synthetic sequences designed for expression in an organism, including, but not limited to, a microorganism or a plant. The compositions also include transformed bacteria, plants, plant cells, tissues, and seeds. Specifically, isolated or recombinant nucleic acid molecules encoding the insecticidal protein-72 (PIP-72) polypeptides of Pseudomonas are provided. In addition, the amino acid sequences corresponding to the PIP-72 polypeptides are included. Isolated or recombinant nucleic acid molecules capable of encoding a PIP-72 polypeptide of sequence number 849 are provided. Furthermore, nucleic acid sequences that are complementary to or hybridize to a nucleic acid sequence of the modalities are covered. They also provide isolated or recombinant PIP-72 polypeptides of sequence with ID number: 849. Methods are provided for producing the PIP-72 polypeptides and silencing elements, and for using those polypeptides and silencing elements to control or kill Lepidoptera, Coleoptera, nematode, fungal, and / or Diptera pests. The transgenic plants of the various embodiments express one or more of the PIP-72 polypeptides and one or more silencing elements. In several embodiments, the transgenic plant further comprises one or more additional genes for insect resistance, for example, one or more additional genes for controlling Coleoptera, Lepidoptera, Hemiptera, or nematode pests. The transgenic plant may further comprise any gene that imparts an agronomic trait of interest. The target silencing polynucleotides or active variants and fragments thereof are provided from U.S. Patent Application Nos. US2014 / 0275208 and US2015 / 0257389. The silencing elements designed with these target nucleotides from U.S. Patent Application Nos. US2014 / 0275208 and US2015 / 0257389 are provided, which, when ingested by the pest, decrease the expression of one or more of the target sequences and thus control the pest (e.g., with insecticidal activity). In one embodiment of the invention, one or more nucleic acid molecules encoding the PIP-72 polypeptides are provided in a molecular stack or expression cassette with one or more silencing elements or silencing objectives described in the publication of U.S. patent application no. US2014 / 0275208 or US2015 / 0257389. The compositions and methods of these strains are useful for producing organisms with greater resistance or tolerance to pests. These organisms and the compositions comprising them are desired for agricultural purposes. BRIEF DESCRIPTION OF THE FIGURES Figure 1 shows a graph depicting the nodal lesion score of the western corn rootworm feeding in TO plants expressing a stacked construct comprising a polynucleotide encoding a PIP-72 polypeptide and the Ryan silencing element (ident. sec. no.: 993) or negative control line, HC69. Figure 2 shows a graph representing the expression in plant T0 of the Ryan silencing element as a stacked construct comprising a polynucleotide encoding a PIP-72 polypeptide and the Ryan silencing element (sequence with ID number: 993) or negative control line, HC69. Figure 3 shows a graph representing the expression at plant T0 of PIP-72 as a stacked construct comprising a polynucleotide encoding a PIP-72 polypeptide and the Ryan silencing element (ident. sec. no.: 993) or negative control line, HC69. DETAILED DESCRIPTION OF THE INVENTION It is understood that this description is not limited to the methodology, protocols, cell lines, genera, and specific reagents described, as these may vary. It is further understood that the terminology used herein is solely for the purpose of describing particular modalities and is not intended to limit the scope of this description. As used in this description, the singular forms “a,” “an,” and “the” include plural referents unless the context clearly indicates otherwise. Thus, for example, the reference to “a cell” includes a plurality of such cells, and the reference to “the proteme” includes the reference to one or more protemes and their equivalents known to those skilled in the art, and so on. All technical and scientific terms used in this description have the same meaning as commonly understood by a person skilled in the art to which this description pertains unless clearly indicated otherwise. This description relates to compositions and methods for pest control. The methods involve the transformation of organisms with nucleic acid sequences encoding a PIP-72 polypeptide and a silencing element or other pesticidal agent as described herein. In particular, the nucleic acid sequences of the Modalities are useful for preparing plants and microorganisms with pesticidal activity. Therefore, transformed bacteria, plants, plant cells, plant tissues, and seeds are provided. The compositions are pesticidal nucleic acids and proteins from bacterial species. The nucleic acid sequences are used in the construction of expression vectors for subsequent transformation into organisms of interest. PIP-72 polypeptides are useful for controlling or exterminating populations of Lepidopteran, Coleoptera, Diptera, Fungi, Hemptera, and Nematode pests and for producing compositions with pesticidal activity. Insect pests of interest include, but are not limited to, Lepidoptera species such as: cabbage moth, e.g., Helicoverpa zea Boddie; soybean looper, e.g., Pseudoplusia includens Walker; and bean velvetbean caterpillar, e.g., Anticarsia gemmatalis Hubner and Coleoptera species including, but not limited to, western corn rootworm (WCR) (Diabrotica virgifera) - WCRW, southern corn rootworm (Diabrotica undecimpunctata howardi) - SCRW, and northern corn rootworm (Diabrotica barberi) - NCRW. “Pesticide proteme” is used in this description to refer to a toxin that has toxic activity against one or more pests, including, but not limited to, members of the orders Lepidoptera, Diptera, Hemiptera, and Coleoptera or the phylum Nematoda, or a proteme that has homology with such protemes. Pesticide protemes have been isolated from organisms that These include, for example, Bacillus sp., Pseudomonas sp., Photorhabdus sp., Xenorhabdus sp., Clostridium bifermentans, and Paenibacillus popilliae. Pesticide proteins include, but are not limited to: insecticidal proteins from Pseudomonas sp. such as PSEEN3174 (Monalysin; (2011) PLoS Pathogens 7:1-13); from the CHA0 and Pf-5 strains of Pseudomonas protegens (formerly fluorescens) (Pechy-Tarr, (2008) Environmental Microbiology 10:2368-2386; GenBank accession number EU400157); of Pseudomonas Taiwanensis (Liu, et al., (2010) J. Agric. Food Chem., 58:12343-12349) and of Pseudomonas pseudoalcligenes (Zhang, et al., (2009) Annals of Microbiology 59:45-50 and Li, et al., (2007) Plant Cell Tiss. Organ Cult. 89:159-168); insecticidal proteins from Photorhabdus sp. and Xenorhabdus sp. (Hinchliffe, et al., (2010) The Open Toxicology Journal, 3:101-118 and Morgan, et al., (2001) Applied and Envir. Micro. 67:2062-2069); US Patent No. 6,048,838, and U.S. patent no. 6,379.946; a PIP-1 polypeptide from U.S. patent serial number 13 / 792861; an AfIP-1A and / or AfIP-1B polypeptide from U.S. patent serial number 13 / 800233; a PHI-4 polypeptide from U.S. patent serial number 13 / 839702; PIP-47 polypeptides from U.S. patent serial number 61 / 866747; the insecticidal proteins from U.S. patent serial numbers 61 / 863761 and 61 / 863763; and 6-endotoxins which include, but are not limited to: the classes Cry1, Cry2, Cry3, Cry4, Cry5, Cry6, Cry7, Cry8, Cry9, Cry10, Cry11, Cry12, Cry13, Cry14, Cry15, Cry16, Cry17, Cry18, Cry19. Cry20, Cry21, Cry22, Cry23, Cry24, Cry25, Cry26, Cry27, Cry 28, Cry 29, Cry 30, Cry31, Cry32, Cry33, Cry34, Cry35, Cry36, Cry37, Cry38, Cry39, Cry40, Cry41, Cry42, Cry43, Cry44, Cry45, Cry 46, Cry47, Cry49, Cry 51, Cry52, Cry 53, Cry 54, Cry55, Cry56, Cry57, Cry58, Cry59. Cry60, Cry61, Cry62, Cry63, Cry64, Cry65, Cry66, Cry67, Cry68, Cry69, Cry70, and Cry71 are 6-endotoxin genes and the cytolytic cyt1 and cyt2 genes of B. thuringiensis. Members of these insecticidal protein classes of B. thuringiensis include, but are not limited to, Cry1Aa1 (accession number AAA22353); Cry1Aa2 (accession number AAA22552); Cry1Aa3 (accession number BAA00257); Cry1Aa4 (accession number CAA31886); Cry1Aa5 (accession number BAA04468); Cry1Aa6 (accession number AAA86265); Cry1Aa7 (accession no. AAD46139); Cry1Aa8 (accession no. I26149); Cry1Aa9 (accession no. BAA77213); Cry1Aa10 (accession no. AAD55382); Cry1Aa11 (accession no. CAA70856); Cry1Aa12 (accession no. AAP80146); Cry1Aa13 (num.access number AAM44305); Cry1Aa14 (access number AAP40639); Cry1Aa15 (access number AAY66993); Cry1Aa16 (access number HQ439776); Cry1Aa17 (access number HQ439788); Cry1Aa18 (access number HQ439790); Cry1Aa19 (access number HQ685121); Cry1Aa20 (access number JF340156); Cry1Aa21 (access number JN651496); Cry1Aa22 (access number KC158223); Cry1Ab1 (access number AAA22330); Cry1Ab2 (access number AAA22613); Cry1Ab3 (accession no. AAA22561); Cry1Ab4 (accession no. BAA00071); Cry1Ab5 (accession no. CAA28405); Cry1Ab6 (order no. accession AAA22420); Cry1Ab7 (accession no. CAA31620); Cry1Ab8 (accession no. AAA22551); Cry1Ab9 (accession no. CAA38701); CrylAblO (accession no. A29125); Cry1Ab11 (accession no. I12419); Cry1Ab12 (accession no. AAC64003); Cry1Ab13 (accession no. AAN76494); Cry1Ab14 (accession no. AAG16877); Cry1Ab15 (accession no. AAO13302); Cry1Ab16 (accession no. AAK55546); Cry1Ab17 (accession no. AAT46415); Cry1Ab18 (accession no. AAQ88259); Cry1Ab19 (accession no. AAW31761); Cry1Ab20 (accession no. ABB72460); Cry1Ab21 (accession no. ABS18384); Cry1Ab22 (accession no. ABW87320); Cry1Ab23 (accession no. HQ439777); Cry1Ab24 (accession no. HQ439778); Cry1Ab25 (accession no. HQ685122); Cry1Ab26 (accession no. HQ847729); Cry1Ab27 (accession no. JN135249); Cry1Ab28 (accession no. JN135250); Cry1Ab29 (accession no. JN135251); Cry1Ab30 (accession no. JN135252); Cry1Ab31 (accession no. JN135253); Cry1Ab32 (accession no. JN135254); Cry1Ab33 (accession no. AAS93798); Cry1Ab34 (accession no.access number KC156668); type Cry1Ab (access number AAK14336); type Cry1Ab (access number AAK14337); type Cry1Ab (access number AAK14338); type Cry1Ab (access number ABG88858); Cry1Ac1 (access number AAA22331); Cry1Ac2 (access number AAA22338); Cry1Ac3 (access number CAA38098); Cry1Ac4 (access number AAA73077); Cry1Ac5 (access number AAA22339); Cry1Ac6 (access number AAA86266); Cry1Ac7 (access number AAB46989); Cry1Ac8 (access number AAC44841); Cry1Ac9 (access number of. lit AAB49768); CrylAclO (accession no. CAA05505); CrylAcll (accession no. CAA10270); Cry1Ac12 (accession no. I12418); Cry1Ac13 (accession no. AAD38701); Cry1Ac14 (accession no. AAQ06607); Cry1Ac15 (accession no. AAN07788); Cry1Ac16 (accession no. AAU87037); Cry1Ac17 (accession number AAX18704); Cry1Ac18 (accession number AAY88347); Cry1Ac19 (accession no. ABD37053); Cry1Ac20 (accession number ABB89046); Cry1Ac21 (accession number AAY66992); Cry1Ac22 (accession no. ABZ01836); Cry1Ac23 (accession no. CAQ30431); Cry1Ac24 (accession no. ABL01535); Cry1Ac25 (accession number FJ513324); Cry1Ac26 (accession number FJ617446); Cry1Ac27 (accession number FJ617447); Cry1Ac28 (accession number ACM90319); Cry1Ac29 (accession number DQ438941); Cry1Ac30 (accession no. GQ227507); Cry1Ac31 (accession number GU446674); Cry1Ac32 (accession no. HM061081); Cry1Ac33 (accession number GQ866913); Cry1Ac34 (accession no. HQ230364); Cry1Ac35 (accession no. JF340157); Cry1Ac36 (no.accession no. JN387137); Cry1Ac37 (accession no. JQ317685); Cry1Ad1 (accession no. AAA22340); Cry1Ad2 (accession no. CAA01880); Cry1Ae1 (accession no. AAA22410); Cry1Af1 (accession no. AAB82749); Cry1Ag1 (accession no. AAD46137); Cry1Ah1 (accession no. AAQ14326); Cry1Ah2 (accession no. ABB76664); Cry1Ah3 (accession no. HQ439779); Cry1Ai1 (accession no. AAO39719); Cry1Ai2 (accession no. HQ439780); Cry1A type (accession no. AAK14339); Cry1Ba1 (accession no. CAA29898); Cry1Ba2. (access number CAA65003); Cry1Ba3 (access number AAK63251); Cry1Ba4 (access number AAK51084); Cry1Ba5 (access number ABO20894); Cry1Ba6 (access number ABL60921); Cry1Ba7 (access number HQ439781); Cry1Bb1 (access number AAA22344); Cry1Bb2 (access number HQ439782); Cry1Bc1 (access number CAA86568); Cry1Bd1 (access number AAD10292); Cry1Bd2 (access number AAM93496); Cry1Be1 (access number AAC32850); Cry1Be2 (access number AAQ52387); Cry1Be3 (access number ACV96720); Cry1Be4 (access number HM070026); Cry1Bf1 (access number CAC50778); Cry1Bf2 (access number AAQ52380); Cry1Bg1 (access number AAO39720); Cry1Bh1 (access number HQ589331); Cry1Bi1 (access number KC156700); Cry1Ca1 (access number CAA30396); Cry1Ca2 (access number CAA31951); Cry1Ca3 (access number AAA22343); Cry1Ca4 (access number CAA01886); Cry1Ca5 (access number CAA65457); Cry1Ca6 [1] (access number AAF37224); Cry1Ca7 (accession no. AAG50438); Cry1Ca8 (accession no. AAM00264); Cry1Ca9 (num.accession no. AAL79362); Cry1Ca10 (accession no. AAN16462); Cry1Ca11 (accession no. AAX53094); Cry1Ca12 (accession no. HM070027); Cry1Ca13 (accession no. HQ412621); Cry1Ca14 (accession no. JN651493); Cry1Cb1 (accession no. M97880); Cry1Cb2 (accession no. AAG35409); Cry1Cb3 (accession no. ACD50894); Cry1Cb type (accession no. AAX63901); Cry1Da1 (accession no. CAA38099); Cry1Da2 (accession no. I76415); Cry1Da3 (accession no. HQ439784); Cry1Db1 (accession no. access CAA80234); Cry1Db2 (access no. AAK48937); CrylDcl (access no. ABK35074); CrylEal (access no. CAA37933); Cry1Ea2 (access no. CAA39609); Cry1Ea3 (access no. AAA22345); Cry1Ea4 (access no. AAD04732); Cry1Ea5 (access no. A15535); Cry1Ea6 (access no. AAL50330); Cry1Ea7 (access no. AAW72936); Cry1Ea8 (access no. ABX11258); Cry1Ea9 (access no. HQ439785); Cry1Ea10 (access no. ADR00398); Cry1Ea11 (accession no. JQ652456); Cry1Eb1 (accession no. AAA22346); Cry1Fa1 (accession no. AAA22348); Cry1Fa2 (accession no. AAA22347); Cry1Fa3 (accession no. HM070028); Cry1Fa4 (accession no. HM439638); Cry1Fb1 (accession no. CAA80235); Cry1Fb2 (accession no. BAA25298); Cry1Fb3 (accession no. AAF21767); Cry1Fb4 (accession no. AAC10641); Cry1Fb5 (accession no. AAO13295); Cry1Fb6 (accession no. ACD50892); Cry1Fb7 (accession no. ACD50893); Cry1Ga1 (accession no. CAA80233); Cry1Ga2 (accession no. CAA70506); Cry1Gb1 (num.access number AAD10291); Cry1Gb2 (access number AAO13756); Cry1Gc1 (access number AAQ52381); Cry1Ha1 (access number CAA80236); Cry1Hb1 (access number AAA79694); Cry1Hb2 (access number HQ439786); type Cry1H (access number AAF01213); Cry1Ia1 (access number CAA44633); Cry1Ia2 (access number AAA22354); Cry1Ia3 (access number AAC36999); Cry1Ia4 (access number AAB00958); Cry1Ia5 (access number CAA70124); Cry1Ia6 (access number AAC26910); Cry1Ia7 (accession no. AAM73516); Cry1Ia8 (num. Cry1la11 (access number AAK66742); Cry1la19 (access number AAQ08616); CryllalO (access number AAP86782); Cryllall (access number CAC85964); Cry1la12 (access number AAV53390); Cry1la13 (access number ABF83202); Cry1la14 (access number ACG63871); Cry1la15 (access number FJ617445); Cry1la16 (access number FJ617448); Cry1la17 (access number GU989199); Cry1la18 (access number ADK23801); Cry1la19 (access number HQ439787); Cry1la20 (access number JQ228426); Cry1la21 (accession no. JQ228424); Cry1la22 (accession no. JQ228427); Cry1la23 (accession no. JQ228428); Cry1la24 (accession no. JQ228429); Cry1la25 (accession no. JQ228430); Cry1la26 (accession no. JQ228431); Cry1la27 (accession no. JQ228432); Cry1la28 (accession no. JQ228433); Cry1la29 (accession no. JQ228434); Cry1la30 (accession no. JQ317686); Cry1la31 (accession no. JX944038); Cry1la32 (accession no. JX944039); Cry1la33 (access number JX944040); Cry1lb1 (access number AAA82114); Cry1lb2 (access numberaccess number ABW88019); Cry1lb3 (access number ACD75515); Cry1lb4 (access number HM051227); Cry1lb5 (access number HM070028); Cry1lb6 (access number ADK38579); Cry1lb7 (access number JN571740); Cry1lb8 (access number JN675714); Cry1lb9 (access number JN675715); Cry1lb10 (access number JN675716); Cry1lb11 (access number JQ228423); Cry1lc1 (access number AAC62933); Cry1lc2 (access number AAE71691); Cry1ld1 (access number AAD44366); Cry1ld2 (accession no. JQ228422); Cry1le1 (accession no. AAG43526); Cry1le2 (accession no. HM439636); Cry1le3 (num. access number KC156647); Cry1Ie4 (access number KC156681); Cryllfl (access number AAQ52382); Cryllgl (access number KC156701); type Cry1I (access number AAC31094); type Cry1I (access number ABG88859); Cry1Ja1 (access number AAA22341); Cry1Ja2 (access number HM070030); Cry1Ja3 (access number JQ228425); Cry1Jb1 (access number AAA98959); Cry1Jc1 (access number AAC31092); Cry1Jc2 (access number AAQ52372); Cry1Jd1 (access number CAC50779); Cry1Ka1 (access number AAB00376); Cry1Ka2 (access number HQ439783); Cry1La1 (access number AAS60191); Cry1La2 (access number HM070031); Cry1Ma1 (access number FJ884067); Cry1Ma2 (access number KC156659); Cry1Na1 (access number KC156648); Cry1Nb1 (access number KC156678); Cry1 type (access number AAC31091); Cry2Aa1 (access number AAA22335); Cry2Aa2 (access number AAA83516); Cry2Aa3 (access number D86064); Cry2Aa4 (access number AAC04867); Cry2Aa5 (access no. CAA10671); Cry2Aa6 (access no. CAA10672); Cry2Aa7 (access no.access number CAA10670); Cry2Aa8 (access number AAO13734); Cry2Aa9 (access number AAO13750); Cry2Aa10 (access number AAQ04263); Cry2Aa11 (access number AAQ52384); Cry2Aa12 (access number ABI83671); Cry2Aa13 (access number ABL01536); Cry2Aa14 (access number ACF04939); Cry2Aa15 (access number JN426947); Cry2Ab1 (access number AAA22342); Cry2Ab2 (access number CAA39075); Cry2Ab3 (access number AAG36762); Cry2Ab4 (access number AAO13296); Cry2Ab5 (accession no. AAQ04609);. Cry2Ab6 (access number AAP59457); Cry2Ab7 (access number AAZ66347); Cry2Ab8 (access number ABC95996); Cry2Ab9 (access number ABC74968); Cry2Ab10 (access number EF157306); Cry2Ab11 (access number CAM84575); Cry2Ab12 (access number ABM21764); Cry2Ab13 (access number ACG76120); Cry2Ab14 (access number ACG76121); Cry2Ab15 (access number HM037126); Cry2Ab16 (access number GQ866914); Cry2Ab17 (access number HQ439789); Cry2Ab18 (access number JN135255); Cry2Ab19 (access number JN135256); Cry2Ab20 (access number JN135257); Cry2Ab21 (access number JN135258); Cry2Ab22 (access number JN135259); Cry2Ab23 (access number JN135260); Cry2Ab24 (access number JN135261); Cry2Ab25 (access number JN415485); Cry2Ab26 (access number JN426946); Cry2Ab27 (access number JN415764); Cry2Ab28 (access number JN651494); Cry2Ac1 (access number CAA40536); Cry2Ac2 (access number AAG35410); Cry2Ac3 (access number AAQ52385); Cry2Ac4 (access number ABC95997); Cry2Ac5 (access numberaccess number ABC74969); Cry2Ac6 (access number ABC74793); Cry2Ac7 (access number CAL18690); Cry2Ac8 (access number CAM09325); Cry2Ac9 (access number CAM09326); Cry2Ac10 (access number ABN15104); Cry2Ac11 (access number CAM83895); Cry2Ac12 (access number CAM83896); Cry2Ad1 (access number AAF09583); Cry2Ad2 (access number ABC86927); Cry2Ad3 (access number CAK29504); Cry2Ad4 (access number CAM32331); Cry2Ad5 (access number CAO78739); Cry2Ae1 (access number. AAQ52362); Cry2Af1 (access number ABO30519); Cry2Af2 (access number GQ866915); Cry2Ag1 (access number ACH91610); Cry2Ah1 (access number EU939453); Cry2Ah2 (access number ACL80665); Cry2Ah3 (access number GU073380); Cry2Ah4 (access number KC156702); Cry2Ai1 (access number FJ788388); Cry2Aj (access number); Cry2Ak1 (access number KC156660); Cry2Ba1 (access number KC156658); Cry3Aa1 (access number AAA22336); Cry3Aa2 (access number AAA22541); Cry3Aa3 (access number CAA68482); Cry3Aa4 (access number AAA22542); Cry3Aa5 (access number AAA50255); Cry3Aa6 (access number AAC43266); Cry3Aa7 (access number CAB41411); Cry3Aa8 (access number AAS79487); Cry3Aa9 (access number AAW05659); Cry3Aa10 (access number AAU29411); Cry3Aa11 (access number AAW82872); Cry3Aa12 (access number ABY49136); Cry3Ba1 (access number CAA34983); Cry3Ba2 (access number CAA00645); Cry3Ba3 (access number JQ397327); Cry3Bb1 (access no. AAA22334); Cry3Bb2 (access no. AAA74198); Cry3Bb3 (access no.accession number I15475); Cry3Ca1 (accession number CAA42469); Cry4Aa1 (accession number CAA68485); Cry4Aa2 (accession number BAA00179); Cry4Aa3 (accession number CAD30148); Cry4Aa4 (accession number AFB18317); type Cry4A (accession number AAY96321); Cry4Ba1 (accession number CAA30312); Cry4Ba2 (accession number CAA30114); Cry4Ba3 (accession number AAA22337); Cry4Ba4 (accession number BAA00178); Cry4Ba5 (accession number CAD30095); type Cry4Ba (accession number ABC47686); Cry4Ca1 (accession number EU646202); Cry4Cb1. (access number FJ403208); Cry4Cb2 (access number FJ597622); Cry4Cc1 (access number FJ403207); Cry5Aa1 (access number AAA67694); Cry5Ab1 (access number AAA67693); Cry5Ac1 (access number I34543); Cry5Ad1 (access number ABQ82087); Cry5Ba1 (access number AAA68598); Cry5Ba2 (access number ABW88931); Cry5Ba3 (access number AFJ04417); Cry5Ca1 (access number HM461869); Cry5Ca2 (access number ZP_04123426); Cry5Da1 (access number HM461870); Cry5Da2 (access number ZP_04123980); Cry5Ea1 (access number HM485580); Cry5Ea2 (access number ZP_04124038); Cry6Aa1 (access number AAA22357); Cry6Aa2 (access number AAM46849); Cry6Aa3 (access number ABH03377); Cry6Ba1 (access number AAA22358); Cry7Aa1 (access number AAA22351); Cry7Ab1 (access number AAA21120); Cry7Ab2 (access number AAA21121); Cry7Ab3 (access number ABX24522); Cry7Ab4 (access number EU380678); Cry7Ab5 (access number ABX79555); Cry7Ab6 (access number ACI44005); Cry7Ab7 (access number ADB89216); Cry7Ab8 (access numberaccess number GU145299); Cry7Ab9 (access number ADD92572); Cry7Ba1 (access number ABB70817); Cry7Bb1 (access number KC156653); Cry7Ca1 (access number ABR67863); Cry7Cb1 (access number KC156698); Cry7Da1 (access number ACQ99547); Cry7Da2 (access number HM572236); Cry7Da3 (access number KC156679); Cry7Ea1 (access number HM035086); Cry7Ea2 (access number HM132124); Cry7Ea3 (access number EEM19403); Cry7Fa1 (access number HM035088); Cry7Fa2 (access number) EEM19090); Cry7Fb1 (access number HM572235); Cry7Fb2 (access number KC156682); Cry7Ga1 (access number HM572237); Cry7Ga2 (access number KC156669); Cry7Gb1 (access number KC156650); Cry7Gc1 (access number access no. KC156654); Cry7Gd1 (access no. KC156697); Cry7Ha1 (access no. access number KC156651); Cry7Ia1 (access number KC156665); Cry7Ja1 (access number access number KC156671); Cry7Ka1 (access number KC156680); Cry7Kb1 (access number access number BAM99306); Cry7La1 (access number BAM99307); Cry8Aa1 (access number AAA21117); Cry8Ab1 (access number EU044830); Cry8Ac1 (access number KC156662); Cry8Ad1 (access number KC156684); Cry8Ba1 (access number AAA21118); Cry8Bb1 (access number CAD57542); Cry8Bc1 (access number CAD57543); Cry8Ca1 (access number AAA21119); Cry8Ca2 (access number AAR98783); Cry8Ca3 (access number EU625349); Cry8Ca4 (access number ADB54826); Cry8Da1 (access number BAC07226); Cry8Da2 (access number BD133574); Cry8Da3 (access number BD133575); Cry8Db1 (access number BAF93483); Cry8Ea1 (access number AAQ73470); Cry8Ea2 (access number EU047597); Cry8Ea3 (access number KC855216); Cry8Fa1 (access number AAT48690); Cry8Fa2 (access number HQ174208); Cry8Fa3 (access number AFH78109); Cry8Ga1 (access number AAT46073); Cry8Ga2 (access number ABC42043); Cry8Ga3 (access number FJ198072); Cry8Ha1 (access number AAW81032); Cry8Ia1 (accession no. EU381044); Cry8Ia2 (num.access GU073381); Cry8Ia3 (access no. HM044664); Cry8Ia4 (access no. KC156674); Cry8Ib1 (access number GU325772); Cry8Ib2 (access number KC156677); Cry8Ja1 (access number EU625348); Cry8Ka1 (access number FJ422558); Cry8Ka2 (access number ACN87262); Cry8Kb1 (access number HM123758); Cry8Kb2 (access number KC156675); Cry8La1 (access number GU325771); Cry8Ma1 (access number HM044665); Cry8Ma2 (access number EEM86551); Cry8Ma3 (access number HM210574); Cry8Na1 (access number HM640939); Cry8Pa1 (access number HQ388415); Cry8Qa1 (access number HQ441166); Cry8Qa2 (access number KC152468); Cry8Ra1 (access number AFP87548); Cry8Sa1 (access number JQ740599); Cry8Ta1 (access number KC156673); Cry8 type (access number FJ770571); Cry8 type (access number ABS53003); Cry9Aa1 (access number CAA41122); Cry9Aa2 (access number CAA41425); Cry9Aa3 (access number GQ249293); Cry9Aa4 (access number GQ249294); Cry9Aa5 (access no. JX174110); type Cry9Aa (access no. AAQ52376); Cry9Ba1 (access no. CAA52927); Cry9Ba2 (access no.accession no. GU299522); Cry9Bb1 (accession no. AAV28716); Cry9Ca1 (accession no. CAA85764); Cry9Ca2 (accession no. AAQ52375); Cry9Da1 (accession no. BAA19948); Cry9Da2 (accession no. AAB97923); Cry9Da3 (accession no. GQ249293); Cry9Da4 (accession no. GQ249297); Cry9Db1 (accession no. AAX78439); Cry9Dc1 (accession no. KC156683); Cry9Ea1 (accession no. BAA34908); Cry9Ea2 (accession no. AAO12908); Cry9Ea3 (accession no. ABM21765); Cry9Ea4 (accession no. ACE88267); Cry9Ea5 (accession no. ACF04743); Cry9Ea6 (accession no. ACG63872); Cry9Ea7 (accession no. FJ380927); Cry9Ea8 (accession no. GQ249292); Cry9Ea9 (accession no. JN651495); Cry9Eb1 (accession no. CAC50780); Cry9Eb2 (accession no. GQ249298); Cry9Eb3 (accession no. KC156646); Cry9Ec1 (accession no. AAC63366); Cry9Ed1 (accession no. AAX78440); Cry9Ee1 (accession no. GQ249296); Cry9Ee2 (accession no. KC156664); Cry9Fa1 (accession no. KC156692); Cry9Ga1 (accession number KC156699); type Cry9 (accession number AAC63366); Cry10Aa1 (accession no. AAA22614); Cry10Aa2 (accession number E00614); Cry10Aa3 (accession number CAD30098); Cry10Aa4 (accession no. AFB18318); type Cry10A (accession number DQ167578); Cry11Aa1 (accession no. AAA22352); Cry11Aa2 (accession number AAA22611); Cry11Aa3 (accession number CAD30081); Cry11Aa4 (accession no. AFB18319); type Cry11Aa (accession number DQ166531); Cry11Ba1 (accession number CAA60504); Cry11Bb1 (accession no. AAC97162); Cry11Bb2 (accession no.access number HM068615); Cry12Aa1 (access number AAA22355); Cry13Aa1 (access number AAA22356); Cry14Aa1 (access number AAA21516); Cry14Ab1 (access number KC156652); Cry15Aa1 (access number AAA22333); Cry16Aa1 (access number CAA63860); Cry17Aa1 (access number CAA67841); Cry18Aa1 (access number CAA67506); Cry18Ba1 (access number AAF89667); Cry18Ca1 (access number AAF89668); Cry19Aa1 (access number CAA68875); Cry19Ba1 (access number BAA32397); Cry19Ca1 (accession number). AFM37572); Cry20Aa1 (access number AAB93476); Cry20Ba1 (access number ACS93601); Cry20Ba2 (access number KC156694); type Cry20 (access number GQ144333); Cry21Aa1 (access number I32932); Cry21Aa2 (access number I66477); Cry21Ba1 (access number BAC06484); Cry21Ca1 (access number JF521577); Cry21Ca2 (access number KC156687); Cry21Da1 (access number JF521578); Cry22Aa1 (access number I34547); Cry22Aa2 (access number CAD43579); Cry22Aa3 (access number ACD93211); Cry22Ab1 (access number AAK50456); Cry22Ab2 (access number CAD43577); Cry22Ba1 (access number CAD43578); Cry22Bb1 (access number KC156672); Cry23Aa1 (access number AAF76375); Cry24Aa1 (access number AAC61891); Cry24Ba1 (access number BAD32657); Cry24Ca1 (access number CAJ43600); Cry25Aa1 (access number AAC61892); Cry26Aa1 (access number AAD25075); Cry27Aa1 (access number BAA82796); Cry28Aa1 (access number AAD24189); Cry28Aa2 (access number AAG00235); Cry29Aa1 (access number CAC80985); Cry30Aa1 (access numberaccess number CAC80986); Cry30Ba1 (access number BAD00052); Cry30Ca1 (access number BAD67157); Cry30Ca2 (access number ACU24781); Cry30Da1 (access number EF095955); Cry30Db1 (access number BAE80088); Cry30Ea1 (access number ACC95445); Cry30Ea2 (access number FJ499389); Cry30Fa1 (access number ACI22625); Cry30Ga1 (access number ACG60020); Cry30Ga2 (access number HQ638217); Cry31Aa1 (access number BAB11757); Cry31Aa2 (accession number AAL87458); Cry31Aa3 (access number BAE79808); Cry31Aa4 (access number BAF32571); Cry31Aa5 (access number BAF32572); Cry31Aa6 (access number BAI44026); Cry31Ab1 (access number BAE79809); Cry31Ab2 (access number BAF32570); Cry31Ac1 (access number BAF34368); Cry31Ac2 (access number AB731600); Cry31Ad1 (access number BAI44022); Cry32Aa1 (access number AAG36711); Cry32Aa2 (access number GU063849); Cry32Ab1 (access number GU063850); Cry32Ba1 (access number BAB78601); Cry32Ca1 (access number BAB78602); Cry32Cb1 (access number KC156708); Cry32Da1 (access number BAB78603); Cry32Ea1 (access number GU324274); Cry32Ea2 (access number KC156686); Cry32Eb1 (access number KC156663); Cry32Fa1 (access number KC156656); Cry32Ga1 (access number KC156657); Cry32Ha1 (access number KC156661); Cry32Hb1 (access number KC156666); Cry32Ia1 (access number KC156667); Cry32Ja1 (access number KC156685); Cry32Ka1 (access number KC156688); Cry32La1 (access number KC156689); Cry32Ma1 (access numberaccess number KC156690); Cry32Mb1 (access number KC156704); Cry32Na1 (access number KC156691); Cry32Oa1 (access number KC156703); Cry32Pa1 (access number KC156705); Cry32Qa1 (access number KC156706); Cry32Ra1 (access number KC156707); Cry32Sa1 (access number KC156709); Cry32Ta1 (access number KC156710); Cry32Ua1 (access number KC156655); Cry33Aa1 (access number AAL26871); Cry34Aa1 (access number AAG50341); Cry34Aa2 (number of. access AAK64560); Cry34Aa3 (access number AAT29032); Cry34Aa4 (access number AAT29030); Cry34Ab1 (access number AAG41671); Cry34Ac1 (access number AAG50118); Cry34Ac2 (access number AAK64562); Cry34Ac3 (access number AAT29029); Cry34Ba1 (access number AAK64565); Cry34Ba2 (access number AAT29033); Cry34Ba3 (access number AAT29031); Cry35Aa1 (access number AAG50342); Cry35Aa2 (access number AAK64561); Cry35Aa3 (access number AAT29028); Cry35Aa4 (accession no. AAT29025); Cry35Ab1 (accession no. AAG41672); Cry35Ab2 (accession no. AAK64563); Cry35Ab3 (accession no. AY536891); Cry35Ac1 (accession no. AAG50117); Cry35Ba1 (accession no. AAK64566); Cry35Ba2 (accession no. AAT29027); Cry35Ba3 (accession no. AAT29026); Cry36Aa1 (accession no. AAK64558); Cry37Aa1 (accession no. AAF76376); Cry38Aa1 (accession no. AAK64559); Cry39Aa1 (accession no. BAB72016); Cry40Aa1 (accession no. BAB72018); Cry40Ba1 (accession no. BAC77648); Cry40Ca1 (num.access number EU381045); Cry40Da1 (access number ACF15199); Cry41Aa1 (access number BAD35157); Cry41Ab1 (access number BAD35163); Cry41Ba1 (access number HM461871); Cry41Ba2 (access number ZP_04099652); Cry42Aa1 (access number BAD35166); Cry43Aa1 (access number BAD15301); Cry43Aa2 (access number BAD95474); Cry43Ba1 (access number BAD15303); Cry43Ca1 (access number KC156676); Cry43Cb1 (access number KC156695); Cry43Cc1 (accession number KC156696); type Cry43. (accession no. BAD15305); Cry44Aa (accession no. BAD08532); Cry45Aa (accession no. BAD22577); Cry46Aa (accession no. BAC79010); Cry46Aa2 (accession no. BAG68906); Cry46Ab (accession no. BAD35170); Cry47Aa (accession no. AAY24695); Cry48Aa (accession no. CAJ18351); Cry48Aa2 (accession no. CAJ86545); Cry48Aa3 (accession no. CAJ86546); Cry48Ab (accession no. CAJ86548); Cry48Ab2 (accession no. CAJ86549); Cry49Aa (accession no. CAH56541); Cry49Aa2 (accession no. CAJ86541); Cry49Aa3 (accession no. CAJ86543); Cry49Aa4 (accession no. CAJ86544); Cry49Ab1 (accession no. CAJ86542); Cry50Aa1 (accession no. BAE86999); Cry50Ba1 (accession number GU446675); Cry50Ba2 (accession number GU446676); Cry51Aa1 (accession no. ABI14444); Cry51Aa2 (accession number GU570697); Cry52Aa1 (accession number EF613489); Cry52Ba1 (accession number FJ361760); Cry53Aa1 (accession number EF633476); Cry53Ab1 (accession number FJ361759); Cry54Aa1 (accession no. ACA52194); Cry54Aa2 (no.access number GQ140349); Cry54Ba1 (access number GU446677); Cry55Aa1 (access number ABW88932); Cry54Ab1 (access number JQ916908); Cry55Aa2 (access number AAE33526); Cry56Aa1 (access number ACU57499); Cry56Aa2 (access number GQ483512); Cry56Aa3 (access number JX025567); Cry57Aa1 (access number ANC87261); Cry58Aa1 (access number ANC87260); Cry59Ba1 (access number JN790647); Cry59Aa1 (access number ACR43758); Cry60Aa1 (accession number ACU24782); Cry60Aa2 (access number EAO57254); Cry60Aa3 (access number EEM99278); Cry60Ba1 (access number GU810818); Cry60Ba2 (access number EAO57253); Cry60Ba3 (access number EEM99279); Cry61Aa1 (access number HM035087); Cry61Aa2 (access number HM132125); Cry61Aa3 (access number EEM19308); Cry62Aa1 (access number HM054509); Cry63Aa1 (access number BAI44028); Cry64Aa1 (access number BAJ05397); Cry65Aa1 (access number HM461868); Cry65Aa2 (access number ZP_04123838); Cry66Aa1 (access number HM485581); Cry66Aa2 (access number ZP_04099945); Cry67Aa1 (access number HM485582); Cry67Aa2 (access number ZP_04148882); Cry68Aa1 (access number HQ113114); Cry69Aa1 (access number HQ401006); Cry69Aa2 (access number JQ821388); Cry69Ab1 (access number JN209957); Cry70Aa1 (access number JN646781); Cry70Ba1 (access number ADO51070); Cry70Bb1 (accession no. EEL67276); Cry71Aa1 (accession no. JX025568); Cry72Aa1 (num.accession number JX025569); Cyt1Aa (gene bank accession number X03182); Cyt1Ab (gene bank accession number X98793); Cyt1B (gene bank accession number U37196); Cyt2A (gene bank accession number Z14147); and Cyt2B (gene bank accession number U52043). Examples of 6-endotoxins also include, but are not limited to, Cry1A proteins of U.S. patents 5,880,275 and 7,858,849, 8,530,411, 8,575,433, and 8,686,233; a DIG-3 or DIG-11 toxin (N-terminal deletion of the a-helix 1 and / or a-helix 2 variants of Cry proteins such as Cry1A, Cry3A) from U.S. patents 8,304,604, 8,304,605 ​​and 8,476,226; CrylB from U.S. patent application serial number 10 / 525,318; CrylC from U.S. patent no. 6,033,874; Cry1F from U.S. patents 5,188,960 and 6,218,188; Cry1A / F chimeras from U.S. patents 7,070,982; 6,962,705 and 6,713,063); a Cry2 protein such as the Cry2Ab protein of U.S. patent no. 7,064,249); a Cry3A protein including, but not limited to, a genetically modified hybrid insecticidal protein (eHIP) created by fusing unique combinations of variable regions and conserved blocks from at least two different Cry proteins (U.S. patent application publication no. 2010 / 0017914); a Cry4 protein; a Cry5 protein; a Cry6 protein; Cry8 proteins of U.S. patents nos. 7,329,736, 7,449,552, 7,803,943, 7,476,781, 7,105,332, 7.378,499 and 7,462,760; a Cry9 proteme such as members of the Cry9A, Cry9B, Cry9C, Cry9D, Cry9E, and Cry9F families, including, but not limited to, the Cry9D proteme of U.S. Patent No. 8,802,933 and the Cry9B proteme of U.S. Patent No. 8,802,934; a Cry15 proteme of Naimov, et al., (2008) Applied and Environmental Microbiology, 74:7145-7151; a Cry22 proteme, a Cry34Ab1 proteme of U.S. Patent Nos. 6,127,180, 6,624,145, and 6,340,593; a CryET33 and CryET34 protein from U.S. patents Nos. 6,248,535, 6,326,351, 6,399,330, 6,949,626, 7,385,107 and 7,504,229; homologues of CryET33 and CryET34 from the. U.S. patent publications no. 2006 / 0191034, 2012 / 0278954 and PCT publication no. WO 2012 / 139004; a Cry35Ab1 protein from U.S. patents no. 6,083,499, 6,548,291 and 6,340,593; a Cry46 protein, a Cry51 protein, a Cry binary toxin; a TIC807 from the publication of U.S. patent application no. 2008 / 0295207; ET29, ET37, TIC809, TIC810, TIC812, TIC127, TIC128 from PCT patent no. US 2006 / 033867; TIC853 toxins from U.S. patent 8,513,494; TIC3131, TIC 3400, and TIC3407 from U.S. patent application publication no. 2015 / 0047076; AXMI-027, AXMI-036, and AXMI-038 from U.S. patent no. 8,236,757; AXMI-031, AXMI-039, AXMI-040, AXMI-049 from U.S. patent no. 7,923,602; AXMI-018, AXMI-020, and AXMI-021 from patent no. WO 2006 / 083891; AXMI-010 from patent no. WO 2005 / 038032; AXMI-003 of patent no. WO 2005 / 021585; AXMI-008 of the publication of the U.S. patent application.No. 2004 / 0250311; AXMI-006 of the publication of U.S. patent application No. 2004 / 0216186; AXMI-007 of the publication of U.S. patent application No. 2004 / 0210965; AXMI-009 of U.S. patent application No. 2004 / 0210964; AXMI-014 of the publication of U.S. patent application No. 2004 / 0197917; AXMI-004 of the publication of U.S. patent application No. 2004 / 0197916; AXMI-028 and AXMI-029 of patent No. 2006 / 119457; AXMI-007, AXMI-008, AXMI-0080rf2, AXMI-009, AXMI-014 and AXMI-004 of patent no. WO 2004 / 074462; AXMI-150 of the patent of the. US No. 8,084,416; AXMI-205 of the patent application publication of U.S. patent application no. 2011 / 0023184; AXMI-011, AXMI-012, AXMI-013, AXMI-015, AXMI-019, AXMI-044, AXMI-037, AXMI-043, AXMI-033, AXMI-034, AXMI-022, AXMI-023, AXMI-041, AXMI-063 and AXMI-064 of U.S. patent application publication no. 2011 / 0263488; AXMI-R1 and related proteins of U.S. patent application publication no. 2010 / 0197592; AXMI221Z, AXMI222z, AXMI223z, AXMI224z and AXMI225z of patent no. WO 2011 / 103248; AXMI218, AXMI219, AXMI220, AXMI226, AXMI227, AXMI228, AXMI229, AXMI230 and AXMI231 of patent no. WO 2011 / 103247 and U.S. patent no. 8,759,619; AXMI-115, AXMI-113, AXMI-005, AXMI-163 and AXMI-184 of U.S. Patent No. 8,334,431; AXMI-001, AXMI-002, AXMI-030, AXMI-035 and AXMI-045 of the publication of U.S. patent application no. 2010 / 0298211; AXMI-066 and AXMI-076 from the publication of U.S. patent application no. 2009 / 0144852 AXMI128, AXMI143, AXMI154, AXMI166, AXMI173, AXMI180, AXMI130, AXMI144, AXMI155, AXMI167, AXMI174, AXMI181, AXMI131, AXMI146, AXMI156, AXMI168, AXMI175, AXMI182, AXMI133, AXMI148, AXMI157, AXMI169, AXMI176, AXMI185, AXMI140, AXMI149, AXMI158, AXMI170, AXMI177, AXMI186, AXMI141, AXMI152, AXMI162, AXMI171, AXMI178, AXMI187, AXMI142 AXMI153 AXMI165 AXMI172 AXMI179 AXMI188 AXMI189 de la patente de los EE. UU. num. 8.318.900; AXMI079, AXMI080, AXMI081, AXMI082, AXMI091, AXMI092, AXMI096, AXMI097, AXMI098, AXMI099, AXMI100, AXMI101, AXMI102, AXMI103, AXMI104, AXMI107, AXMI108, AXMI109, AXMI110, AXMI111, AXMI112, AXMI114, AXMI116, AXMI117, AXMI118, AXMI119, AXMI120, AXMI121, AXMI122, AXMI123, AXMI124, AXMI1257, AXMI1268, AXMI127, AXMI129, AXMI164, AXMI151, AXMI161, AXMI183, AXMI132, AXMI138, AXMI137 of U.S. patent application publication no. 2010 / 0005543, AXMI270 of U.S. patent application publication US20140223598, AXMI279 of U.S. patent application publication 20140223599, cry proteins such as CryA and Cry3A having modified proteolytic sites of U.S. patent no. 8,319,019; a Cry1Ac, Cry2Aa and Cry1Ca toxin protein of the VBTS 2528 strain of Bacillus thuringiensis of U.S. patent application publication no. 2011 / 0064710. Other Cry proteins are well known to an expert in the field (see, Crickmore, et al., “Bacillus thuringiensis toxin nomenclature” (2011), in lifesci.sussex.ac.uk / home / Neil_Crickmore / Bt / , which can be accessed on the internet using the prefix “www”). The insecticidal activity of Cry proteins is well known to someone skilled in the field (for a review, see van Frannkenhuyzen, (2009) J. Invert. Path. 101:1-16). Someone skilled in the field is familiar with the use of Cry proteins as traits in transgenic plants and with Cry transgenic plants, which include, but are not limited to, plants expressing Cry1Ac, Cry1Ac+Cry2Ab, Cry1Ab, Cry1A.105, Cry1F, Cry1Fa2, Cry1F+Cry1Ac, Cry2Ab, Cry3A, mCry3A, Cry3Bb1, Cry34Ab1, Cry35Ab1, Vip3A, mCry3A, Cry9c, and CBI-Bt have received regulatory approval (see Sanahuja, (2011) Plant Biotech Journal 9:283-300 and the CERA GM Crop Database (2010) of the Center for Environmental Risk Assessment (CERA), ILSI Research Foundation, Washington DC at cera-gmc.org / index.php?action=gm_crop_database, accessible via the internet using the prefix “www”). More than one known pesticide protein may also be expressed in plants such as Vip3Ab & Cry1Fa (US2012 / 0317682); Cry1BE & Cry1F (US2012 / 0311746); Cry1CA & Cry1AB (US2012 / 0311745); Cry1F & CryCa (US2012 / 0317681); Cry1DA & Cry1BE (US2012 / 0331590); Cry1DA & Cry1Fa (US2012 / 0331589); Cry1AB & Cry1BE (US2012 / 0324606); Cry1Fa & Cry2Aa and Cry1I & Cry1E (US2012 / 0324605); Cry34Ab / 35Ab and Cry6Aa (US20130167269); Cry34Ab / VCry35Ab & Cry3Aa (US patent application no.US20130167268); Cry1Ab & Cry1F (US20140182018); and Cry3A and Cry1Ab or Vip3Aa (US20130116170). Pesticide proteins also include insecticidal lipases, including lipid acyl hydrolases of U.S. patent no. 7,491,869, and cholesterol oxidases such as those from Streptomyces (Purcell et al. (1993) Biochem Biophys Res Commun 15:1406-1413). Pesticide proteins also include VIP toxins (vegetative insecticidal proteins) of U.S. patent no. 5,877,012, 6,107,279, 6,137,033, 7,244,820, 7,615,686, and 8,237,020, and the like. Other VIP protemes are well known to an expert in the field (see,). lifesci.sussex.ac.uk / home / Neil_Crickmore / Bt / vip.html, which can be accessed on the internet using the prefix “www”). Pesticide proteins also include toxin complex (TC) proteins, which can be obtained from organisms such as Xenorhabdus, Photorhabdus, and Paenibacillus (see U.S. Patent Nos. 7,491,698 and 8,084,418). Some TC proteins have “independent” insecticidal activity, and other TC proteins enhance the activity of independent toxins produced by the same organism. The toxicity of an “independent” TC protein (from Photorhabdus, Xenorhabdus, or Paenibacillus, for example) can be increased by one or more “enhancer” TC proteins derived from a source organism of a different genus. There are three main types of TC proteins. As referred to in this description, Class A proteins (“Protein A”) are independent toxins.Class B proteins (“Protein B”) and Class C proteins (“Protein C”) increase the toxicity of Class A proteins. Examples of Class A proteins are TcbA, TcdA, XptAI, and XptA2. Examples of Class B proteins are TcaC, TcdB, XptBIXb, and XptCIWi. Examples of Class C proteins are TccC, XptCIXb, and XptBIWi. Pesticide proteins also include proteins from spider, snake, and scorpion venom. Examples of spider venom peptides include, but are not limited to, lycotoxin-1 peptides and mutants thereof (U.S. Patent No. 8,334,366). One aspect refers to isolated or recombinant nucleic acid molecules comprising nucleic acid sequences encoding PIP-72 polypeptides and a silencing element. As used herein, the term “nucleic acid molecule” refers to DNA molecules (e.g., recombinant DNA, cDNA, genomic DNA, plastid DNA, mitochondrial DNA) and RNA molecules (e.g., mRNA) and DNA or RNA analogs generated by the use of nucleotide analogs. The nucleic acid molecule may be single-stranded or double-stranded, but is preferably double-stranded DNA. An “isolated” nucleic acid (or DNA) molecule is used herein to refer to a nucleic acid (or DNA) sequence that is no longer found in its natural environment, e.g., in vitro. A “recombinant” nucleic acid (or DNA) molecule is used herein to refer to a nucleic acid (or DNA) sequence that is in a recombinant bacterial or plant host cell. In some embodiments, an “isolated” or “recombinant” nucleic acid is free of sequences (preferably protein-coding sequences) that naturally flank the nucleic acid (i.e., sequences located at the 5' and 3' ends of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For the purposes of this description, “isolated” or “recombinant,” when used to refer to nucleic acid molecules, excludes isolated chromosomes.For example, in several forms, the recombinant nucleic acid molecule that encodes a PIP-72 polypeptide may contain. less than approximately 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb or 0.1 kb of nucleic acid sequences that naturally flank the nucleic acid molecule in the genomic DNA of the cell from which the nucleic acid is derived. In some forms, an isolated nucleic acid molecule encoding a PIP-72 polypeptide has one or more nucleic acid sequence changes compared to the native or genomic nucleic acid sequence. In some forms, the change in the native or genomic nucleic acid sequences includes, but is not limited to: changes in the nucleic acid sequence due to genetic code degeneracy; changes in the nucleic acid sequence due to substitution, insertion, deletion, and / or addition of amino acids compared to the native or genomic sequence; deletion of one or more introns; deletion of one or more upstream or downstream regulatory regions; and deletion of the 5' and / or 3' untranslated region associated with the genomic nucleic acid sequence. In some forms, the nucleic acid molecule that encodes a PIP-72 polypeptide is a non-genomic sequence.The polynucleotide sources that encode the PIP-72 polypeptides include but are not limited to sec. with ident. no.: 1, sec. with ident. no.: 3, sec. with ident. no.: 5, sec. with ident. no.: 7, sec. with ident. no.: 9, sec. with ident. no.: 11, sec. with ident. no.: 13, sec. with ident. no.: 17, sec. with ident. no.: 27 and sec. with ident. no.: 31, sec. with ident. no.: 949, sec. with ident. no.: 950. sec. with ident. no.: 955, sec. with ident. no.: 956, sec. with ident. no.: 957, sec. with ident. no.: 958, sec. with ident. no.: 961, sec. with ident. no.: 962, sec. with ident. no.: 963, sec. with ident. no.: 965, sec. with ident. no.: 966, sec. with ident. no.: 967, and sec. with ident. no.: 968. Examples of PIP-72 polypeptide sequences that can be used to obtain the sequences encoding the corresponding nucleotides include, but are not limited to, the PIP-72 polypeptides of sec. with number ID: 2, sec. with number of ident.: 4, sec. with number ID: 6, sec. with number ID: 8, sec. with number ID: 10, sec. with number of ident.: 12, sec. with number of ident.: 14, sec. with number of ident.: 18, sec. with number of ident.: 28 and sec. with number of ident.: 32, sec. with number of ident.: 927, sec. with number of ident.: 928, sec. with number of ident.: 932, sec. with number of ident.: 933, sec. with number of ident.: 934, sec. with number of ident.: 935, sec. with ident. no.: 936, sec. with ident. no.: 939, sec. with ident. no.: 940, sec. with ident. no.: 941, sec. with ident. no.: 943, sec. with ident. no.: 944, sec. with ident. no.: 945, or sec. with ident. no.: 946. The modalities encompass nucleic acid molecules that are fragments of these nucleic acid sequences encoding the PIP-72 polypeptides and a silencing element. “Fragment,” as used herein, refers to a portion of the nucleic acid sequence encoding a PIP-72 polypeptide and / or a silencing element. A fragment of a nucleic acid sequence can encode a portion. Biologically active from a PIP-72 polypeptide or a silencing element, or it may be a fragment that can be used as a hybridization probe or PCR primer by using the methods described below. Nucleic acid molecules that are fragments of a nucleic acid sequence encoding a PIP-72 polypeptide or a silencing element comprise at least approximately 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, or 260 contiguous nucleotides, or up to the number of nucleotides present in a full-length nucleic acid sequence encoding a PIP-72 polypeptide or a silencing element described herein, depending on the intended use. “Contiguous nucleotides” is used in this description to refer to nucleotide residues that are immediately adjacent to one another.Fragments of the nucleic acid sequences of the modality will encode protein fragments or silencing elements that retain biological activity and, therefore, retain insecticidal activity. “Retains activity” is used herein to refer to a polypeptide or silencing element that has at least approximately 10%, at least approximately 30%, at least approximately 50%, at least approximately 70%, 80%, 90%, 95%, or higher of the insecticidal activity of the full-length nucleic acid or polypeptide sequence. In one modality, the insecticidal activity is against Lepidoptera. against a species of beetle. In one embodiment, the insecticidal activity is against a Diabrotica species. In one embodiment, the insecticidal activity is against one or more insect pests of the corn rootworm complex: corn leafworm, Diabrotica virgifera virgifera; northern corn rootworm, D. barberi; southern corn rootworm; cucumber spotted beetle, Diabrotica undecimpunctata howardi; and Mexican corn rootworm, D. virgifera zeae. In one embodiment, the insecticidal activity is against the western corn rootworm, Diabrotica virgifera virgifera. In some models, sequence identity is calculated using the ClustalW algorithm in the ALIGNX® module of the Vector NTI® software (Invitrogen Corporation, Carlsbad, Calif.) with all parameters predefined. In some models, sequence identity is calculated along the entire length of the polypeptide using ClustalW in the ALIGNX® module of the Vector NTI software (Invitrogen Corporation, Carlsbad, Calif.) with all parameters predefined. To determine the percentage of identity between two amino acid sequences or two nucleic acid sequences, the sequences are aligned for optimal comparison. The percentage of identity between the two sequences is a function of the number of identical positions shared by the sequences (i.e., percentage of identity = number of identical positions / total number of positions (e.g., overlapping positions) * 100). In one modality, the two sequences have the same length. In another modality, the comparison is made over the entire reference sequence (e.g., the entire sec. with ID number 1, sec. with ID number 2). The percentage of identity between two sequences can be determined using techniques similar to those described below, allowing or not allowing breaks. When calculating the percentage of identity, exact matches are typically counted. The determination of the percentage identity between two sequences can be obtained using a mathematical algorithm. A non-limiting example of a mathematical algorithm used for comparing two sequences is the algorithm of Karlin and Altschul (1990) Proc. Natl. Acad. Sci. USA 87:2264, modified as in Karlin and Altschul (1993) Proc. Natl. Acad. Sci. USA 90:5873-5877. Such an algorithm is incorporated into the BLASTN and BLASTX programs of Altschul et al. (1990) J. Mol. Biol. 215:403. BLAST nucleotide searches can be performed with the BLASTN program, score=100, word length=12, to obtain nucleic acid sequences homologous to pesticide nucleic acid molecules of the modalities. BLAST protein searches can be carried out with the BLASTX program, score=50, word length=3, to obtain amino acid sequences homologous to pesticide protein molecules of the modalities.To obtain break alignments for comparative purposes, Gapped BLAST (in BLAST 2.0) can be used as shown. This is described in Altschul et al. (1997) Nucleic Acids Res. 25:3389. Alternatively, PSI-Blast can be used to perform a repeated search that detects distant relationships between molecules. See Altschul et al. (1997) above. When using the BLAST, Gapped BLAST, and PSI-Blast programs, the default parameters of the respective programs can be used (e.g., BLASTX and BLASTN). Alignment can also be performed manually for inspection. Another non-limiting example of a mathematical algorithm used for sequence comparison is the ClustalW algorithm (Higgins et al., (1994) Nucleic Acids Res. 22:4673-4680). The ClustalW program compares sequences and aligns the entire amino acid or DNA sequence and can therefore provide data on sequence conservation within the complete amino acid sequence. The ClustalW algorithm is used in several commercially available DNA / amino acid analysis software packages, such as the ALIGNX® module of the Vector NTI® software package (Invitrogen Corporation, Carlsbad, Calif.). After aligning amino acid sequences with the ClustalW program, it is possible to evaluate the percentage of amino acid identity. A non-limiting example of a useful software program for analyzing ClustalW alignments is GENEDOC™.GENEDOC™ (Karl Nicholas) allows the evaluation of amino acid (or DNA) similarity and identity between multiple proteins. This is another non-limiting example of a mathematical algorithm used for sequence comparison. This is the algorithm of Myers and Miller, (1988) CABIOS 4:11-17. This algorithm is incorporated into the ALIGN program (version 2.0), which is part of the GCG Wisconsin Genetics software package, version 10 (available from Accelrys, Inc., 9685 Scranton Rd., San Diego, Calif., USA). When using the ALIGN program to compare amino acid sequences, a residue weight table of PAM120, a break length penalty of 12, and a break penalty of 4 can be used. Another non-limiting example of a mathematical algorithm used for sequence comparison is the Needleman and Wunsch algorithm (1970) J. Mol. Biol. 48(3):443-453, using GAP Version 10 software to determine sequence identity or similarity using the following predefined parameters: % identity and % similarity for a nucleic acid sequence using a break weight of 50 and a length weight of 3 and the nwsgapdna.cmpii scoring matrix; % identity or % similarity for an amino acid sequence using a break weight of 8 and a length weight of 2, and the BLOSUM62 scoring program. Equivalent programs may also be used.“Equivalent program” is used in this description to refer to any sequence comparison program that, for any pair of sequences in question, generates an alignment that has identical amino acid residue matches and an identical percentage of identity. sequence when compared to the corresponding alignment generated by GAP Version 10. The variants also include nucleic acid molecules that encode variants of the PIP-72 polypeptide and a silencing element. “Variants” of the nucleic acid sequences described herein include those sequences that differ conservatively due to degeneration of the genetic code as well as those that are sufficiently identical, as described above. Naturally occurring allelic variants can be identified using well-known molecular biology techniques, such as polymerase chain reaction (PCR) and hybridization techniques summarized below. Nucleic acid sequence variants also include synthetically generated nucleic acid sequences, such as those produced by site-directed mutagenesis, that still encode the PIP-72 polypeptides described below. Descriptions of various procedures for generating diversity in modified nucleic acid sequences, for example, those encoding polypeptides with pesticidal activity or fragments thereof, can be found in the following publications, and the references are cited in this description: Soong, et al., (2000) Nat Genet 25(4):436-439; Stemmer, et al., (1999) Tumor Targeting 4:1-4; Ness, et al., (1999) Nat Biotechnol 17:893-896; Chang, et al., (1999) Nat Biotechnol 17:793 797; Minshull and Stemmer, (1999) Curr Opin Chem Biol 3:284-290; Christians, et al., (1999) Nat Biotechnol 17:259-264; Crameri, et al., (1998) Nature 391:288291; Crameri, et al., (1997) Nat Biotechnol 15:436-438; Zhang, et al., (1997) PNAS USA 94:4504-4509; Patten, et al., (1997) Curr Opin Biotechnol 8:724-733; Crameri, et al., (1996) Nat Med 2:100-103; Crameri, et al., (1996) Nat Biotechnol 14:315-319; Gates, et al., (1996) J Mol Biol 255:373-386; Stemmer, (1996) “Sexual PCR and Assembly PCR” In: The Encyclopedia of Molecular Biology. VCH Publishers, New York. pags. 447-457; Crameri and Stemmer, (1995) BioTechniques 18:194-195; Stemmer, et al., (1995) Gene, 164:49-53; Stemmer, (1995) Science 270: 1510; Stemmer, (1995) Bio / Technology 13:549-553; Stemmer, (1994) Nature 370:389-391 and Stemmer, (1994) PNAS USA 91:1074710751. Mutational methods for generating diversity include, for example, site-directed mutagenesis (Ling, et al., (1997) Anal Biochem 254(2):157-178; Dale, et al., (1996) Methods Mol Biol 57:369-374; Smith, (1985) Ann Rev Genet 19:423-462; Botstein and Shortle, (1985) Science 229:1193-1201; Carter, (1986) Biochem J 237:1-7 and Kunkel, (1987) “The efficiency of oligonucleotide directed mutagenesis” in Nucleic Acids & Molecular Biology (Eckstein and Lilley, eds., Springer Verlag, Berlin)); mutagenesis using uracil-containing templates (Kunkel, (1985) PNAS USA 82:488-492; Kunkel, et al., (1987) Methods Enzymol 154:367-382 and Bass, et al., (1988) Science 242:240-245); directed oligonucleotide mutagenesis (Zoller and Smith, (1983) Methods Enzymol 100:468-500; Zoller y Smith, (1987) Methods Enzymol 154:329-350 (1987); Zoller y Smith, (1982) Nucleic Acids Res 10:6487-6500), phosphorothioate-modified DNA mutagenesis (Taylor, et al., (1985) Nucl Acids Res 13:8749-8764; Taylor, et al., (1985) Nucl Acids Res 13:8765-8787 (1985); Nakamaye y Eckstein, (1986) Nucl Acids Res 14:9679-9698; Sayers, et al., (1988) Nucl Acids Res 16:791-802 y Sayers, et al., (1988) Nucl Acids Res 16:803-814); mutagenesis mediante el uso de ADN bicatenario incomplete (Kramer, et al., (1984) Nucl Acids Res 12:9441-9456; Kramer y Fritz, (1987) Methods Enzymol 154:350-367; Kramer, et al., (1988) Nucl Acids Res 16:7207 y Fritz, et al., (1988) Nucl Acids Res 16:6987-6999). Additional suitable methods include mismatch repair (Kramer, et al., (1984) Cell 38:879-887), mutagenesis using repair-deficient host strains (Carter, et al., (1985) Nucl Acids Res 13:4431-4443 and Carter, (1987) Methods in Enzymol 154:382-403), deletion mutagenesis (Eghtedarzadeh and Henikoff, (1986) Nucl Acids Res 14:5115), restriction-selection and restriction-purification (Wells, et al., (1986) Phil Trans R Soc Lond A 317:415-423), mutagenesis by total gene synthesis (Nambiar, et al., (1984) Science 223:1299-1301; Sakamar and Khorana, (1988) Nucl Acids Res 14:6361-6372; Wells, et al., (1985) Gene 34:315-323 and Grundstrom, et al., (1985) Nucl Acids Res 13:3305-3316), repair of the double-strand break (Mandecki, (1986) PNAS USA, 83:7177-7181 and Arnold, (1993) Curr Opin Biotech 4:450-455). Details Additional information on many of the above methods can be found in Methods Enzymol Vol. 154, which also describes useful controls for troubleshooting various mutagenesis methods. Additional details regarding various diversity generation methods can be found in the following U.S. patents, PCT publications, and EPO applications and publications: U.S. patent no. 5,723,323, U.S. patent no. 5,763,192, U.S. patent no. US patent no. 5,814,476 and US patent no. 5,817,483 US patent no. 5,824,514 and US patent no. 5,976,862 US patent no. 5,605,793 and US patent no. 5,811,238 US patent no. 5,830,721 and US patent no. 5,834,252 number 5,837,458, WO 1995 / 22625, WO 1996 / 33207, WO 1997 / 20078, WO 1997 / 35966, WO 1999 / 41402, WO 1999 / 41383, WO 1999 / 41369, WO 1999 / 41368, EP 752008, EP 0932670, WO 1999 / 23107, WO 1999 / 21979, WO 1998 / 31837, WO 1998 / 27230, WO 1998 / 27230, WO 2000 / 00632, WO 2000 / 09679, WO 1998 / 42832, WO 1999 / 29902, WO 1998 / 41653, WO 1998 / 41622, WO 1998 / 42727, WO 2000 / 18906, WO 2000 / 04190, WO 2000 / 42561, WO 2000 / 42559, WO 2000 / 42560, WO 2001 / 23401 and PCT / US01 / 06775. The nucleotide sequences of the modalities can also be used, to isolate the corresponding sequences from other organisms. In this way, methods such as PCR, hybridization, and others can be used. Similarly, to identify these sequences based on their sequence homology with the sequences described herein. Sequences selected based on their sequence identity with the complete sequences described herein, or with fragments thereof, are covered in the modalities. These sequences include sequences that are orthologs of the described sequences. The term “orthologs” refers to genes derived from a common ancestral gene and found in different species as a result of speciation. Genes found in different species are considered orthologs when their nucleotide sequences and / or their encoded protein sequences share substantial identity, as defined elsewhere in this description. Frequently, the functions of orthologs are highly conserved across species. In a PCR approach, primer oligonucleotides can be designed for use in PCR reactions to amplify the corresponding DNA sequences from cDNA or genomic DNA extracted from any organism of interest. Methods for designing PCR primers and PCR cloning are generally known in the field and are described in Sambrook et al. (1989) Molecular Cloning: A Laboratory Manual (2nd ed., Cold Spring Harbor Laboratory Press, Plainview, New York), hereafter referred to as “Sambrook.” See also Innis et al., eds. (1990) PCR Protocols: A Guide to Methods and Applications (Academic Press, New York); Innis and Gelfand, eds. (1995) PCR Strategies (Academic Press, New York). Press, New York); and Innis and Gelfand, eds. (1999) PCR Methods Manual (Academic Press, New York). Known PCR methods include, but are not limited to, methods using paired primers, nested primers, specific individual primers, degenerate primers, primers gene-specific, vector-specific primers, primers partially non-coincident, and similar. Alternatively, the protein identification method based on mass spectrometry can be used to identify PIP-72 polypeptide homologs using protocols described in the literature (Scott Patterson, (1998), 10.22, 1-24, Current Protocol in Molecular Biology published by John Wiley & Son Inc.). Specifically, the LC-MS / MS-based protein identification method is used to associate MS data from specific cell lysates or samples enriched with the desired molecular weight (extracted by SDS-PAGE from bands with molecular weight relevant to PIP-72) with information on the sequences of PIP-72 (e.g., sequence number 2)) and its homologs. Any match in the peptide sequences indicates the potential presence of the homologs in the samples. Additional techniques (protein purification and molecular biology) can be used to isolate the protein and identify homologous sequences. In hybridization methods, all or part of the pesticide nucleic acid sequence can be used to analyze genomic or cDNA libraries. Methods for constructing such genomic and cDNA libraries are generally known in the field and are described in Sambrook and Russell (2001), above. The so-called hybridization probes can be fragments of genomic DNA, cDNA fragments, RNA fragments, or other oligonucleotides and can be labeled with a detectable group such as 32P or any other detectable marker, such as other radioisotopes, a fluorescent compound, an enzyme, or an enzyme cofactor. Hybridization probes can be carried out by labeling synthetic oligonucleotides based on the nucleic acid sequence described herein. Degenerate primers designed based on nucleotides or amino acid residues conserved in the nucleic acid sequence or the encoded amino acid sequence can also be used.The probe typically comprises a region of the nucleic acid sequence that hybridizes under rigorous conditions to at least approximately 12, at least approximately 25, at least approximately 50, 75, 100, 125, 150, 175, or 200 consecutive nucleotides of a nucleic acid sequence of the description or a fragment or variant thereof. Methods for the preparation of probes for hybridization are generally known in the field and are described in Sambrook and Russell (2001), above, which is incorporated herein by reference. For example, a complete nucleic acid sequence described herein, or one or more portions thereof, may be used as a probe that It can hybridize specifically to the corresponding nucleic acid sequences encoding the polypeptide-like sequences of PIP-72 and messenger RNA. To achieve specific hybridization under a variety of conditions, such probes include sequences that are unique and are preferably at least approximately 10 nucleotides long or at least approximately 20 nucleotides long. Such probes can be used to amplify the corresponding pesticide sequences by PCR from a selected organism. This technique can be used to isolate additional coding sequences from a desired organism or as a diagnostic assay to determine the presence of coding sequences in an organism. Hybridization techniques include hybridization selection of DNA libraries grown on plates (either in plates or colonies); see, for example, Sambrook, et al., (1989) Molecular Cloning: A Laboratory Manual (2nd ed.)., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY). Hybridization of these sequences can be performed under rigorous conditions. “Rigorous conditions” or “rigorous hybridization conditions” is used herein to refer to conditions under which a probe will hybridize to its target sequence to a detectably greater degree than to other sequences (e.g., at least 2-fold over the background). Rigorous conditions are sequence-dependent and will differ under different circumstances. By controlling the rigor of the hybridization conditions and / or the Under washing conditions, target sequences that are 100% complementary to the probe can be identified (homologous probe). Alternatively, the stringency of the conditions can be adjusted to allow for some sequence mismatch, resulting in the detection of a lower degree of similarity (heterologous probe). Generally, a probe is less than approximately 1000 nucleotides in length, preferably less than 500 nucleotides. Typically, stringent conditions are those in which the salt concentration is less than approximately 1.5 M Na ions, typically with a concentration of approximately 0.01 to 1.0 M sodium ions (or other salts) at a pH of 7.0 to 8.3 and a temperature of at least approximately 30 °C for short probes (e.g., 10 to 50 nucleotides) and at least approximately 60 °C for long probes (e.g., greater than 50 nucleotides). Stringent conditions can also be achieved by adding destabilizing agents such as formamide. Examples of low-stricity conditions include hybridization with a buffer solution of 30 to 35% formamide, 1 M NaCl, 1% SDS (sodium dodecyl sulfate) at 37 °C, and a wash in 1* to 2*SSC (20*ssc = 3.0 m NaCl / 0.3 M trisodium citrate) at 50 to 55 °C. Illustrative moderate-stricity conditions include hybridization in 40 to 45% formamide, 1.0 M NaCl, 1% SDS at 37 °C., and a wash at 0.5* to 1*SSC at 55 to 60 °C. Illustrative high-rigor conditions include. Hybridization in 50% formamide, 1 M NaCl, 1% SDS at 37 °C, and a wash in 0.1*SSC at 60–65 °C. Optionally, the wash buffers may comprise approximately 0.1% to approximately 1% SDS. The duration of hybridization is generally less than approximately 24 hours, usually approximately 4 to approximately 12 hours. Specificity is typically a function of the washes following hybridization; the critical factors are the ionic strength and temperature of the final wash solution. For DNA-DNA hybrids, Tm can be approximately calculated using the equation of Meinkoth and Wahl, (1984) Anal. Biochem. 138:267-284: Tm=81.5 °C+16.6 (log M)+0.41 (% GC)-0.61 (% form)-500 / l; where M is the molarity of monovalent cations, % GC is the percentage of guanosine and cytosine nucleotides in the DNA, % form is the percentage of formamide in the hybridization solution, and L is the length of the hybrid in base pairs. Tm is the temperature (with defined ionic strength and pH) at which 50% hybridization occurs to a complementary target sequence using a perfectly matched probe. Tm is reduced by approximately 1 °C for each 1% mismatch; therefore, Tm, hybridization conditions, and / or washing conditions can be adjusted to hybridize sequences of the desired identity.For example, if searching for sequences with 90% identity, the Tm can be reduced by 10 °C. Generally, the selected rigorous conditions are approximately 5 °C lower than the thermal melting temperature (Tm) for the sequence. specific sequence and its complement to a defined ionic strength and pH. However, very rigorous conditions may use hybridization and / or washing at 1, 2, 3, or 4 °C lower than the thermal melting temperature (Tm); moderately rigorous conditions may use hybridization and / or washing at 6, 7, 8, 9, or 10 °C lower than the thermal melting temperature (Tm); and low-rigor conditions may use hybridization and / or washing at 11, 12, 13, 14, 15, or 20 °C lower than the thermal melting temperature (Tm). By using the equation, the hybridization and washing compositions, and the desired Tm, persons with ordinary knowledge in the field will understand that essentially variations in the rigor of the hybridization and / or washing solutions are being described.If the desired degree of discrepancy results in a Tm lower than 45 °C (aqueous solution) or 32 °C (formamide solution), it is preferable to increase the SSC concentration so that a higher temperature can be used. Extensive guidance on nucleic acid hybridization can be found in Tijssen, (1993) Laboratory Techniques in Biochemistry and Molecular Biology—Hybridization with Nucleic Acid Probes, Part I, Chapter 2 (Elsevier, NY); and Ausubel, et al., eds. (1995) Current Protocols in Molecular Biology, Chapter 2 (Greene Publishing and Wiley-Interscience, New York). See, Sambrook, et al., (1989) Molecular Cloning: A Laboratory Manual (2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY). As used in this description, the terms “protein,” “peptide molecule,” or “polypeptide” include any molecule comprising five or More amino acids. It is well known in the field that protein, peptide, or polypeptide molecules can undergo modifications, including post-translational modifications such as, but not limited to, disulfide bond formation, glycosylation, phosphorylation, or oligomerization. Therefore, as used in this description, the terms “protein,” “peptide molecule,” or “polypeptide” include any protein that is modified by any biological or non-biological process. The terms “amino acid” and “amino acids” refer to all naturally occurring L-amino acids. A “recombinant proteme” is used herein to refer to a proteme that is no longer in its natural environment, for example, in vitro or in a recombinant bacterium or plant host cell. A PIP-72 polypeptide that is substantially free of cellular material includes proteme preparations that have less than approximately 30%, 20%, 10%, or 5% (dry weight) of non-pesticide proteme (furthermore referred to herein as “contaminant proteme”). The term “fragment” refers to a portion of the polynucleotide or a portion of the amino acid sequence and, therefore, to the protein encoded by these. Polynucleotide fragments can encode protein fragments that retain the biological activity of the native protein. Biologically active “fragments” or “portions” include polypeptide fragments comprising amino acid sequences sufficiently identical to a PIP-72 polypeptides exhibit insecticidal activity. Alternatively, polynucleotide fragments that are useful as a silencing element need not encode fragmented proteins that maintain biological activity. Consequently, the fragments of a nucleotide sequence can range from approximately 10, 15, 16, 17, 18, 19 nucleotides, 20, 22, 50, 75, 100, 200, 300, 400, 500, 600, 700 nucleotides, and up to the full-length polynucleotide used.Alternatively, the fragments of a nucleotide sequence can vary from 1-50, 25-75, 75-125, 50-100, 125-175, 175-225, 100-150, 100-300, 150-200, 200-250, 225-275, 275-325, 250-300, 325-375, 375-425, 300-350, 350-400, 425-475, 400-450, 475-525, 450-500, 525-575, 575-625, 550-600, 625-675, 675-725, 600-650, 625-675, 675-725, 650-700, 725-825, 825-875, 750-800, 875-925, 925-975, 850-900, 925-975, 975-1025, 950-1000, 1000-1050, 1025-1075, 1075-1125, 1050-1100, 1125-1175, 1100-1200, 1175-1225, 1225-1275, 1200-1300, 1325-1375, 1375-1425 1300-1400, 1425-1475, 1475-1525, 1400-1500, 1525-1575, 1575-1625, 1625-1675, 1675-1725, 1725-1775, 1775-1825, 1825-1875, 1875-1925, 1925-1975, 1975-2025, 2025-2075, 2075-2125, 2125-2175, 2175-2225, 1500-1600, 1600-1700, 1700-1800, 1800-1900 1900-2000 of the sequences. described herein. A biologically active portion of a PIP-72 polypeptide may be a polypeptide that is, for example, 10, 25, 50, 55, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, or 85 amino acids in length. Such biologically active portions may be prepared by recombinant techniques and evaluated for insecticidal activity. As used herein, a fragment comprises at least eight contiguous amino acids of a PIP-72 polypeptide. In some forms, illustrative PIP-72 polypeptides are described in sec. with ident. no.: 2, sec. with ident. no.: 4, sec. with ident. no.: 6, sec. with ident. no.: 8, sec. with ident. no.: 10, sec. with ident. no.: 12, sec. with ident. no.: 14; Sec. with ident. no.: 18, sec. with ident. no.: 28, sec. with ident. no.: 32, sec. with ident. no.: 528, sec. with ident. no.: 529, sec. with ident. no.: 530, sec. with ident. no. of ident.: 531, sec. with number of ident.: 532, sec. with number of ident.: 533, sec. with number of ident.: 534, sec. with number ID: 535, sec. with number of ident.: 536, sec. with number of ident.: 537, sec. with number of ident.: 538, sec. with number of ident.: 539, sec. with number ID: 540, sec. with number of ident.: 541, sec. with number of ident.: 542, sec. with number of ident.: 543, sec. with number of ident.: 544, sec. with number of ident.: 545, sec. with number of ident.: 546, sec. with number of ident.: 547, sec. with number of id.: 548, sec. with num. of ident.: 549, sec. with num. of ident.: 550, sec. with num. of ident.: 551, sec. with num. of ident.: 552, sec. with num. of ident.: 553, sec. with num. of ident. with num. of ident.: 556, sec. with ident.: 558, sec. with num. of ident. with num. of ident.: 561, sec. with ident.: 563, sec. with num. of ident. with num. of ident.: 566, sec. with ident.: 568, sec. with num. of ident. with num. of ident.: 571, sec. with ident.: 573, sec. with num. of ident. with num. of ident.: 576, sec. with ident.: 578, sec. with num. of ident. with num. of ident.: 581, sec. with ident.: 583, sec. with num. of ident. with num. of ident.: 586, sec. with ident.: 588, sec. with num. of ident. with num. of ident.: 591, sec. with ident.: 593, sec. with num. of ident. with num. of ident.: 596, sec. with ident.: 598, sec. with num. of ident. with num. of ident.: 601, sec. with ident.: 603, sec. with num. of ident. with num. of ident.: 606, sec. with 554, sec. with ident. number: 555, sec. num. of ident.: 557, sec. with num. of 559, sec. with ident. number: 560, sec. num. of ident.: 562, sec. with num. of 564, sec. with ident. number: 565, sec. num. of ident.: 567, sec. with num. of 569, sec. with ident. number: 570, sec. num. of ident.: 572, sec. with num. of 574, sec. with ident. number: 575, sec. num. of ident.: 577, sec. with num. of 579, sec. with ident. number: 580, sec. num. of ident.: 582, sec. with num. of 584, sec. with ident. number: 585, sec. num. of ident.: 587, sec. with num. of 589, sec. with ident. number: 590, sec. num. of ident.: 592, sec. with num. of 594, sec. with ident. number: 595, sec. num. of ident.: 597, sec. with num. of 599, sec. with ident. number: 600, sec. num. of ident.: 602, sec. with num. of 604, sec. with ident. number: 605, sec. num. of ident.: 607, sec. with num. of ident.: 608, sec. with num. of ident. with num. of ident.: 611, sec. with ident.: 613, sec. with num. of ident. with num. of ident.: 616, sec. with ident.: 618, sec. with num. of ident. with num. of ident.: 621, sec. with ident.: 623, sec. with num. of ident. with num. of ident.: 626, sec. with ident.: 628, sec. with num. of ident. with num. of ident. with num. of ident.: 631, sec. with ident.: 633, sec. with num. of ident. with num. of ident.: 636, sec. with ident.: 638, sec. with num. of ident. with num. of ident. with num. of ident.: 641, sec. with ident.: 643, sec. with num. of ident. with num. of ident.: 646, sec. with ident.: 648, sec. with num. of ident. with num. of ident.: 651, sec. with ident.: 653, sec. with num. of ident. with num. of ident.: 656, sec. with ident.: 658, sec. with num. of ident. with num. of ident.: 661, sec. with 609, sec. with ident. number: 610, sec. num. of ident.: 612, sec. with num. of 614, sec. with ident. number: 615, sec. num. of ident.: 617, sec. with num. of 619, sec. with ident. number: 620, sec. num. of ident.: 622, sec. with num. of 624, sec. with ident. number: 625, sec. num. of ident.: 627, sec. with num. of 629, sec. with ident. number: 630, sec. num. of ident.: 632, sec. with num. of 634, sec. with ident. number: 635, sec. num. of ident.: 637, sec. with num. of 639, sec. with ident. number: 640, sec. num. of ident.: 642, sec. with num. of 644, sec. with ident. number: 645, sec. num. of ident.: 647, sec. with num. of 649, sec. with ident. number: 650, sec. num. of ident.: 652, sec. with num. of 654, sec. with ident. number: 655, sec. num. of ident.: 657, sec. with num. of 659, sec. with ident. number: 660, sec. num. of ident.: 662, sec. with num. of ident.: 663, sec. with num. of ident. with num. of ident.: 666, sec. with ident.: 668, sec. with num. of ident. with num. of ident.: 671, sec. with ident.: 673, sec. with num. of ident. with num. of ident.: 676, sec. with ident.: 678, sec. with num. of ident. with num. of ident.: 681, sec. with ident.: 683, sec. with num. of ident. with num. of ident.: 686, sec. with ident.: 688, sec. with num. of ident. with num. of ident.: 691, sec. with ident.: 693, sec. with num. of ident. with num. of ident.: 696, sec. with ident.: 698, sec. with num. of ident. with num. of ident.: 701, sec. with ident.: 703, sec. with num. of ident. with num. of ident.: 706, sec. with ident.: 708, sec. with num. of ident. with num. of ident.: 711, sec. with ident.: 713, sec. with num. of ident. with num. of ident.: 716, sec. with 664, sec. with ident. number: 665, sec. num. of ident.: 667, sec. with num. of 669, sec. with ident. number: 670, sec. num. of ident.: 672, sec. with num. of 674, sec. with num. of ident.: 675, sec. num. of ident.: 677, sec. with num. of 679, sec. with ident. number: 680, sec. num. of ident.: 682, sec. with num. of 684, sec. with ident. number: 685, sec. num. of ident.: 687, sec. with num. of 689, sec. with ident. number: 690, sec. num. of ident.: 692, sec. with num. of 694, sec. with ident. number: 695, sec. num. of ident.: 697, sec. with num. of 699, sec. with num. of ident.: 700, sec. num. of ident.: 702, sec. with num. of 704, sec. with ident. number: 705, sec. num. of ident.: 707, sec. with num. of 709, sec. with ident. number: 710, sec. num. of ident.: 712, sec. with num. of 714, sec. with ident. number: 715, sec. num. of ident.: 717, sec. with num. of ident.: 718, sec. with num. of ident. with num. of ident.: 721, sec. with ident.: 723, sec. with num. of ident. with num. of ident.: 726, sec. with ident.: 728, sec. with num. of ident. with num. of ident.: 731, sec. with ident.: 733, sec. with num. of ident. with num. of ident.: 736, sec. with ident.: 738, sec. with num. of ident. with num. of ident.: 741, sec. with ident.: 743, sec. with num. of ident. with num. of ident.: 746, sec. with ident.: 748, sec. with num. of ident. with num. of ident. with num. of ident.: 751, sec. with ident.: 753, sec. with num. of ident. with num. of ident.: 756, sec. with ident.: 758, sec. with num. of ident. with num. of ident.: 761, sec. with ident.: 763, sec. with num. of ident. with num. of ident.: 766, sec. with ident.: 768, sec. with num. of ident. with num. of ident.: 825, sec. with 719, sec. with ident. number: 720, sec. num. of ident.: 722, sec. with num. of 724, sec. with ident. number: 725, sec. num. of ident.: 727, sec. with num. of 729, sec. with ident. number: 730, sec. num. of ident.: 732, sec. with num. of 734, sec. with ident. number: 735, sec. num. of ident.: 737, sec. with num. of 739, sec. with ident. number: 740, sec. num. of ident.: 742, sec. with num. of 744, sec. with ident. number: 745, sec. num. of ident.: 747, sec. with num. of 749, sec. with ident. number: 750, sec. num. of ident.: 752, sec. with num. of 754, sec. with ident. number: 755, sec. num. of ident.: 757, sec. with num. of 759, sec. with ident. number: 760, sec. num. of ident.: 762, sec. with num. of 764, sec. with ident. number: 765, sec. num. of ident.: 767, sec. with num. of 771, sec. with ident. number: 772, sec. num. of ident.: 826, sec. with num. of ident.: 827, sec. with num. of ident. with num. of ident.: 830, sec. with ident.: 832, sec. with num. of ident. with num. of ident.: 835, sec. with ident.: 837, sec. with num. of ident. with num. of ident. with num. of ident.: 840, sec. with ident.: 842, sec. with num. of ident. with num. of ident.: 852, sec. with ident.: 854, sec. with num. of ident. with num. of ident. with num. of ident.: 857, sec. with ident.: 859, sec. with num. of ident. with num. of ident. with num. of ident.: 862, sec. with ident.: 864, sec. with num. of ident. with num. of ident. with num. of ident.: 905, sec. with ident.: 907, sec. with num. of ident. with num. of ident.: 910, sec. with ident.: 912, sec. with num. of ident. with num. of ident.: 927, sec. with ident.: 932, sec. with num. of ident. with num. of ident.: 935, sec. with ident.: 939, sec. with num. of ident. 828, sec. with ident. number: 829, sec. num. of ident.: 831, sec. with num. of 833, sec. with ident. number: 834, sec. num. of ident.: 836, sec. with num. of 838, sec. with ident. number: 839, sec. num. of ident.: 841, sec. with num. of 843, sec. with ident. number: 844, sec. num. of ident.: 853, sec. with num. of 855, sec. with ident. number: 856, sec. num. of ident.: 858, sec. with num. of 860, sec. with ident. number: 861, sec. num. of ident.: 863, sec. with num. of 903, sec. with ident. number: 904, sec. num. of ident.: 906, sec. with num. of 908, sec. with ident. number: 909, sec. num. of ident.: 911, sec. with num. of 913, sec. with ident. number: 914, sec. num. of ident.: 928, sec. with num. of 933, sec. with ident. number: 934, sec. num. of ident.: 936, sec. with num. of 940, sec. with ident. number: 941, sec. with num. de ident.: 943, sec. with num. de ident.: 944, sec. with num. de ident.: 945 and the sec. with num. de ident.: 946. In some embodiments, a PIP-72 polypeptide has a calculated molecular weight between approximately 6 kDa and approximately 13 kDa, between approximately 7 kDa and approximately 12 kDa, between approximately 8 kDa and approximately 11 kDa, between approximately 9 kDa and approximately 10 kDa, approximately 8.75 kDa, approximately 9 kDa, approximately 9.25 kDa, approximately 9.5 kDa, approximately 9.75 kDa, approximately 10 kDa, approximately 10.25 kDa, and approximately 10.5 kDa. As used herein, the term “approximately” used in the context of the molecular weight of a PIP-72 polypeptide means ± 0.25 kilodaltons. In some embodiments, the PIP-72 polypeptide has a modified physical property. As used herein, the term “physical property” refers to any parameter suitable for describing the physicochemical characteristics of a protein. As used herein, “physical property of interest” and “property of interest” are used interchangeably to refer to physical properties of proteins that are being investigated and / or modified. Examples of physical properties include, but are not limited to, net surface charge and charge distribution on the protein surface, net hydrophobicity and distribution of hydrophobic residues on the protein surface, surface charge density, and density of surface hydrophobicity, total count of ionizable surface groups, Surface tension, protein size and its distribution in solution, melting temperature, heat capacity, and second virial coefficient are examples of physical properties. Examples of physical properties also include, but are not limited to, solubility, folding, stability, and digestibility. In some embodiments, the PIP-72 polypeptide has increased digestibility of proteolytic fragments in the gut of an insect. Models for digestion by simulated gastric fluids are known to those skilled in the field (Fuchs, RL and JD Astwood. Food Technology 50: 83-88, 1996; Astwood, JD, et al Nature Biotechnology 14: 1269-1273, 1996; Fu TJ et al J. Agric Food Chem. 50: 7154-7160, 2002). The term “variants” refers to substantially similar sequences. For polynucleotides, a variant comprises a deletion and / or addition of one or more nucleotides at one or more internal sites within the active polynucleotide and / or a substitution of one or more nucleotides at one or more sites in the native polynucleotide. A polynucleotide variant that is useful as a silencing element will retain the ability to reduce the expression of the target polynucleotide and, in some embodiments, thereby control an insect pest of the plants of interest. As used herein, a “native” polynucleotide or polypeptide comprises a naturally occurring sequence of nucleotides or amino acids, respectively. For polynucleotides, conservative variants include sequences that Due to the degeneration of the genetic code, they encode the amino acid sequence of one of the described polypeptides. Polynucleotide variants also include synthetically generated polynucleotides, such as those produced, for example, using site-directed mutagenesis, but which still retain the desired activity. Generally, variants of a particular described polynucleotide (i.e., a silencing element) will have at least approximately 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more sequence identity with that particular polynucleotide, as determined by the sequence alignment programs and parameters described elsewhere in this description. Variants of a particular described polynucleotide (i.e., the reference polynucleotide) can be further evaluated by comparing the percentage of sequence identity between the polypeptide encoded by a variant of the polynucleotide and the polypeptide encoded by the reference polynucleotide. The percentage of sequence identity between any two polypeptides can be calculated using sequence alignment programs and parameters described elsewhere in this description. If any given pair of described polynucleotides is evaluated by comparing the percentage of sequence identity shared by the two encoding polypeptides, the percentage of sequence identity between the two encoded polypeptides is at least approximately 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or greater sequence identity. In some forms, the variants include polypeptides that differ in amino acid sequence due to mutagenesis. The protein variants covered in the description are biologically active, meaning they still have the desired biological activity (i.e., pesticidal activity) of the native protein. In some forms, the variant will have at least approximately 10%, at least approximately 30%, at least approximately 50%, at least approximately 70%, at least approximately 80% or more of the insecticidal activity of the native protein. In some formulations, the variants may have better activity compared to the native protein. Bacterial genes frequently have multiple methionine start codons close to the beginning of the open reading frame. Often, the initiation of translation at one or more of these start codons will lead to the generation of a functional protein. These start codons may include ATG codons. However, bacteria such as Bacillus sp. also recognize the GTG codon as a start codon, and proteins that initiate translation at GTG codons contain methionine as their first amino acid. Rarely, translation in bacterial systems can be initiated at a TTG codon, although in this case TTG encodes a different protein. methionine. Furthermore, it is frequently not determined a priori which of these codons are naturally used in the bacteria. AsL, it is understood that the use of one of the alternative methionine codons can also lead to the generation of pesticidal proteins. These pesticidal proteins are covered in this description and can be used in the methods described herein. It is understood that, when expressed in plants, it will be necessary to alter the alternative start codon to ATG for proper translation. In another aspect, the PIP-72 polypeptide can be expressed as a precursor protein with an interspersed sequence that catalyzes multi-step post-translational protein splicing. Protein splicing involves the excision of an intermediate sequence from a polypeptide with the simultaneous joining of flanking sequences to produce a new polypeptide (Chong, et al., (1996) J. Biol. Chem., 271:22159-22168).This intercalated sequence or protein splicing element, referred to in this description as internals, catalyzes its own excision through three coordinated reactions at the N-terminal and C-terminal splicing junctions: an acyl rearrangement of the cysteine ​​or N-terminal serine; a transesterification reaction between two terminals to form a branched ester or thioester intermediate; and a peptide bond cleavage coupled to the cyclization of the asparagine at the C-terminal of the internal to release the internal (Evans, et al., (2000) J. Biol. Chem.,. 275:9091-9094. The clarification of the court and defense mechanism has given rise to various international-based applications (Comb, et al., EE. UU. patent number 5,496,714; Comb, et al., EE. UU. patent number 5,834,247; Camarero and Muir, (1999) J. Amer. Soc. 121:55975598; Chong, et al., (1997) Gene 192:271-281, Chong, et al., (1998) 273:1056710577; Cotton, et al., (1999) J. Am. Chem. Soc. 121:1100-1101; Evans, et al., (1999) J. Biol. Chem. 274:18359-18363; Evans, et al., (1999) J. Biol. Chem. 274:3923-3926; Evans, et al., (1998) Protein Sci. 7:2256-2264; Evans, et al., (2000) J. Biol. Chem. 275:9091-9094; Iwai y Pluckthun, (1999) FEBS Lett. 459:166-172; Mathys, et al., (1999) Gene 231:1-13; Mills, et al., (1998) Proc. Natl. Acad. Sci USA 95:3543-3548; Muir, et al., (1998) Proc. Natl. Acad. Sci USA 95:6705-6710; Otomo, et al., (1999) Biochemistry 38:16040-16044; Otomo, et al., (1999) J. Biolmol.NMR 14:105-114; Scott, et al., (1999) Proc. Natl. Acad. Sci. USA 96:13638-13643; Severinov y Muir, (1998) J. Biol. Chem. 273:16205-16209; Shingledecker, et al., (1998) Gene 207:187-195; Southworth, et al., (1998) EMBO J. 17:918-926; Southworth, et al., (1999) Biotechniques 27:110-120; Wood, et al., (1999) Nat. Biotechnology. 17:889-892; Wu, et al., (1998a) Proc. Natl. Acad. Sci. USA 95:9226-9231; Wu, et al., (1998b) Biochim Biophys Acta 1387:422-432; Xu, et al., (1999) Proc. Natl. Acad. Sci. USA 96:388-393; Yamazaki, et al., (1998) J. Am. Chem. Soc., 120:5591-5592). For the application of internal transgenes of plants, worms,. Yang, et al., (Transgene Res 15:583-593 (2006)) y Evans, et al., (Annu. Rev. Plant Biol. 56:375-392 (2005)). In another aspect, the PIP-72 polypeptide can be encoded by two separate genes, where the precursor protein's interna is derived from the two genes and is called the separation interna. The two precursor portions are then joined by the formation of a peptide bond. This peptide bond formation occurs via interna-mediated trans splicing. For this purpose, a first and second expression cassette comprising the two separate genes further encode internas capable of mediating protein trans splicing. Through trans splicing, the proteins and polypeptides encoded by the first and second fragments can be joined by the formation of peptide bonds. Trans splicing internas can be selected from the nuclear and organelle genomes of various organisms, including eukaryotes, archaea, and eubacteria. The internas that can be used are listed at neb.com / neb / inteins.HTML, which can be accessed on the internet using the prefix “www”). The nucleotide sequence encoding an internal protein can be divided into a 5' and a 3' portion that encode the 5' and 3' portions of the internal protein, respectively. Portions of the sequence that are not needed for splicing the internal protein (e.g., homing endonuclease domain) can be removed. The internal protein coding sequence is divided in such a way that the 5' and 3' portions are capable of trans splicing. To select a suitable splicing site of the internal protein... For the internal coding sequence, the considerations published by Southworth, et al., (1998) EMBO J. 17:918-926 should be followed. When constructing the first expression cassette and the second expression cassette, the 5' internal coding sequence is joined to the 3' end of the first fragment encoding the N-terminal part of the PIP-72 polypeptide and the 3' internal coding sequence is joined to the 5' end of the second fragment encoding the C-terminal part of the PIP-72 polypeptide. Generally, trans splice pairs can be designed using any split interna, including any naturally occurring or artificially split interna. Several naturally occurring split internas are known, for example: the split interna of the DnaE gene from Synechocystis sp. PCC6803 (see Wu, et al., (1998) Proc Natl Acad Sci USA. 95(16):9226-31 and Evans, et al., (2000) J Biol Chem. 275(13):9091-4 and the DnaE gene of Nostoc punctiforme (see Iwai, et al., (2006) FEBS Lett. 580(7):1853-8). Undivided internas have been artificially divided in the laboratory to create new divided internas, for example: the artificially divided interna Ssp DnaB (see Wu, et al., (1998) Biochim Biophys Acta. 1387:422-32) and the divided interna Sce VMA (see Brenzel, et al., (2006) Biochemistry. 45(6):1571-8) and a artificially divided fungal mininte^na (see, Elleuche, et al., (2007) Biochem Biophys Res Commun. 355(3):830-4).There are also available internal databases that catalog known internals (see, for example, the online database available at:). bioinformatics.weizmann.ac.il / ~pietro / inteins / inteinstable.html, which can be accessed on the internet using the prefix “www”). Naturally occurring undivided interns may have endonuclease or other enzymatic activities that can typically be eliminated when an artificially divided intern is designed. Such mini-interns or minimized divided interns are well known in the field and are typically less than 200 amino acid residues in length (see Wu et al., (1998) Biochim Biophys Acta. 1387:422-32). Suitable divided interns may have other purifying polypeptide elements added to their structure, provided that these elements do not inhibit splicing of the divided intern or are added in a manner that allows their removal before splicing. Protein splicing has been reported using proteins comprising bacterial interior-like (BIL) domains (see, Amitai, et al., (2003) Mol Microbiol.47:61-73) and self-processing hedgehog (Hog) domains (the latter being combined with inte^nas when referring to the Hog / inte^na superfamily or the HINT family (see, Dassa, et al., (2004) J Biol Chem. 279:320017)) and domains such as these can also be used to prepare artificially spliced ​​inte^nas. In particular, non-splicing members of such families can be modified by molecular biology methodologies to introduce or restore splicing activity in such related species. Recent studies demonstrate that splicing can be observed when a spliced ​​interna component is left in the N-terminus. react with a split internal component at the C-terminus that is not found in nature as a “collaborator” of this internal; for example, splicing has been observed when using collaborators that have as low a homology as 30 to 50% with the “natural” splicing collaborator (see, Dassa, et al., (2007) Biochemistry. 46(1):322-30). Other such mixtures of disparate split internal pairs have been shown to be non-reactive with each other (see, Brenzel, et al., (2006) Biochemistry. 45(6):1571-8). However, it is within the ability of a person skilled in the relevant field to determine whether a particular pair of polypeptides is capable of associating with each other to provide a functional internal, by using routine methods and without the exercise of inventive skills. The development of recombinant DNA methods has made it possible to study the effects of sequence transposition on protein folding, structure, and function. The approach used in creating new sequences resembles that of naturally occurring protein pairs that are related by linear rearrangement of their amino acid sequences (Cunningham, et al., (1979) Proc. Natl. Acad. Sci. USA 76:3218-3222; Teather and Erfle, (1990) J. Bacteriol. 172:3837-3841; Schimming, et al., (1992) Eur. J. Biochem. 204:13-19; Yamiuchi and Minamikawa, (1991) FEBS Lett. 260:127-130; MacGregor, et al., (1996) FEBS Lett. 378:263-266). The first in vitro application of this type of rearrangement to proteins was described by Goldenberg and Creighton (J. Mol. Biol. 165:407-413, 1983). In the creation of a circular permutation variant, a new N-terminal end is selected at an internal site (breakpoint) of the original sequence. The new sequence has the same amino acid order as the original from the breakpoint until it reaches an amino acid at or near the original C-terminal end. At this point, the new sequence joins, either directly or via an additional sequence portion (linker), to an amino acid at or near the original N-terminal end. The new sequence continues with the same sequence as the original until it reaches a point at or near the amino acid that was N-terminal to the breakpoint site of the original sequence. This residue forms the new C-terminal end of the chain.The amino acid sequence length of the linker can be selected either directly or guided by structural information, or by a combination of both approaches. When structural information is unavailable, a small series of linkers can be prepared for evaluation using a design whose lengths are varied to cover a range of 0 to 50 Å and whose sequence is selected to be consistent with surface exposure (hydrophilicity, Hopp and Woods, (1983) Mol. Immunol. 20:483-489; Kyte and Doolittle, (1982) J. Mol. Biol. 157:105-132; solvent-exposed surface area, Lee and Richards, (1971) J. Mol. Biol. 55:379-400) and the ability to adopt the required conformation without disrupting the polypeptide configuration. pesticide (conformationally flexible; Karplus and Schulz, (1985) Naturwissenschaften 72:212-213). The assumption of an average translation of 2.0 to 3.8 A per residue means that the average length to be evaluated will be between 0 and 30 residues, with a preferred range of 0 to 15 residues. Illustrative of such empirical series would be to construct linkers by using a cassette sequence such as Gly-Gly-Gly-Ser repeated n times, where n is 1, 2, 3, or 4. Experts in the field will recognize that there are many such sequences that vary in length or composition that can serve as linkers, with the primary consideration being that they are neither excessively long nor short (cf., Sandhu, (1992) Critical Rev. Biotech.12:437-462); If they are too long, the effects of entropy will probably destabilize the three-dimensional folding and may also make folding kinetically impractical, and if they are too short, they will probably destabilize the molecule due to torsional or steric strain. Experts in the analysis of structural protein information will recognize that the distance between the ends of the chain, defined as the distance between the c-alpha carbons, can be used to define the length of the sequence to be used or at least to limit the number of possibilities that must be evaluated in an empirical selection of linkers. They will also recognize that sometimes the positions of the ends of the polypeptide chain are not well defined in structural models derived from x-ray diffraction data. Nuclear magnetic resonance spectroscopy, and when these are true, it will therefore be necessary to take this situation into account to adequately estimate the required linker length. From the residues whose positions are well defined, two residues close in sequence to the ends of the chain are selected, and the distance between their c-alpha carbons is used to calculate an approximate length for a linker between them. Using the calculated length as a guide, linkers are then selected within a range of residue numbers (calculated using 2 to 3.8 Å per residue).These linkers can be composed of the original sequence, shortened or lengthened as needed. When lengthened, the additional residues can be chosen to be flexible and hydrophilic, as described above. Alternatively, the original sequence can be replaced with a series of linkers, an example being the Gly-Gly-Gly-Ser cassette method mentioned earlier. A combination of the original sequence and a new sequence of suitable overall length can also be used. Pesticide polypeptide sequences capable of folding into biologically active states can be prepared by appropriately selecting the initial (amino-terminal end) and final (carboxy-terminal end) positions within the original polypeptide chain using the linker sequence described above. The amino- and carboxy-terminal ends are selected within a span. A common sequence, called a breakpoint region, is created using the instructions described below. A new amino acid sequence is thus generated by selecting the amino and carboxyl termini within the same breakpoint region. In many cases, the selection of the new termini will be such that the original position of the carboxyl terminus immediately precedes that of the amino terminus. However, experts in the field will recognize that termini selections anywhere within the region can work, and that these will effectively lead to deletions or additions in the amino or carboxyl portions of the new sequence. It is a central principle of molecular biology that the primary amino acid sequence of a protein determines its folding into the three-dimensional structure necessary for the expression of its biological function.Experts in the field are familiar with methods for obtaining and interpreting three-dimensional structural information using X-ray diffraction of individual protein crystals or nuclear magnetic resonance spectroscopy of protein solutions. Examples of structural information relevant to identifying breakpoint regions include the location and type of secondary structure of the protein (alpha and 3-10 helices, parallel and antiparallel beta sheets, chain inversions and turns, and circuits; Kabsch and Sander, (1983) Biopolymers 22:2577-2637); the degree of solvent exposure of residues. amino acids, the extent and type of residue interactions between residues (Chothia, (1984) Ann. Rev. Biochem. 53:537-572), and the static and dynamic distribution of conformations along the polypeptide chain (Alber and Mathews, (1987) Methods Enzymol. 154:511-533). In some cases, additional information is known about residue exposure to the solvent; an example is a post-translational carbohydrate binding site that is necessarily on the protein surface. When structural information is unavailable or not feasible to obtain, methods are also available to analyze the primary amino acid sequence to make predictions about the protein's tertiary and secondary structure, solvent accessibility, and the occurrence of turns and loops.Sometimes, biochemical methods are also applicable for the empirical determination of surface exposure when direct structural methods are not feasible; for example, by using the identification of chain cleavage sites after limited proteolysis to infer surface exposure (Gentile and Salvatore, (1993) Eur. J. Biochem. 218:603-621). Therefore, using experimentally obtained structural information or predictive methods (e.g., Srinivisan and Rose, (1995) Proteins: Struct., Funct. & Genetics 22:81-99), the parental amino acid sequence is inspected to classify regions according to whether or not they are essential for the maintenance of secondary and tertiary structure. The presence of sequences within regions known to be essential is also considered. Regions involved in periodic secondary structure (alpha and 3-10 helices, parallel and antiparallel beta sheets) are regions that should be avoided. Similarly, amino acid sequence regions that are observed or predicted to have a low degree of solvent exposure are more likely to be part of the so-called hydrophobic core of the protein and should also be avoided for the selection of amino- and carboxy-terminal ends. In contrast, regions known or predicted to be in surface turns or loops, and especially regions known to be necessary for biological activity, are the preferred sites for polypeptide chain end location. Continuous stretches of amino acid sequence that are preferred based on the above criteria are called a breakpoint region.Polynucleotides encoding the circular permuted PIP-72 polypeptides with a new N-terminus / C-terminus containing a linker region separating the original C-terminus and N-terminus can be fabricated essentially by following the method described in Mullins et al. (1994) J. Am. Chem. Soc. 116:5529-5533. Multiple steps of polymerase chain reaction (PCR) amplification are used to rearrange the DNA sequence encoding the primary amino acid sequence of the protein. produced according to the tandem duplication method described in Horlick, et al., (1992) Protein Eng. 5:427-431. Polymerase chain reaction (PCR) amplification of genes with new N-terminal / C-terminal ends is performed using a tandemly duplicated DNA template. The methods for designing and constructing fusion proteins (and the polynucleotides that encode them) are well known to experts in the field. Polynucleotides encoding a PIP-72 polypeptide can be fused to signal sequences that direct the localization of the PIP-72 polypeptide to particular compartments of a prokaryotic or eukaryotic cell and / or direct the secretion of the PIP-72 polypeptide from a prokaryotic or eukaryotic cell. For example, in E. coli, it may be desirable to direct protein expression to the periplasmic space. Examples of signal sequences or proteins (or fragments thereof) to which the PIP-72 polypeptide can fuse to direct polypeptide expression to the periplasmic space of bacteria include, but are not limited to, the pelB signal sequence, the maltose-binding protein (MBP) signal sequence, MBP, the ompA signal sequence, the E signal sequence.periplasmic coli and the alkaline phosphatase signal sequence. Several vectors are commercially available for the construction of fusion proteins that direct the localization of a protein, such as the pMAL series of vectors (particularly the pMAL-p series) available from New England Biolabs® (240 County Road, Ipswich, MA 01938-2723). In one modality. Specifically, the polypeptide PIP-72 can be fused to the pectate lyase pelB signal sequence to increase the efficiency of expression and purification of such polypeptides in Gram-negative bacteria (see U.S. Patent Nos. 5,576,195 and 5,846,818). Plant plastid transit peptide / polypeptide fusions are well known in the field (see U.S. Patent No. 7,193,133). Apoplast transit peptides, such as alpha-amylase secretion signals from rice or barley, are also well known in the field. The plastid transit peptide is generally fused to the N-terminal end of the target polypeptide (e.g., the fusion pair). In one embodiment, the fusion protein essentially consists of the plastid-to-transit peptide and the PIP-72 polypeptide to be treated. In another embodiment, the fusion protein comprises the plastid-to-transit peptide and the polypeptide to be targeted.In these embodiments, the plastid transit peptide is preferentially located at the N-terminus of the fusion protein. However, additional amino acid residues may be found at the N-terminus of the plastid transit peptide as long as the fusion protein is at least partially directed to a plastid. In one specific embodiment, the plastid transit peptide is located at the N-terminus half, one-third of the N-terminus, or one-quarter of the N-terminus of the fusion protein. Most or all of the plastid transit peptide is generally cleaved from the fusion protein after insertion into the plastid. As a result, the cleavage site may vary slightly among plant species and at different stages of plant development. of specific intercellular conditions or the particular combination of transit peptide / fusion partner used. In one embodiment, the cleavage of the plastid transit peptide is homogeneous, such that the cleavage site is identical in a population of fusion proteins. In another embodiment, the plastid transit peptide is not homogeneous, such that the cleavage site varies by 1–10 amino acids in a population of fusion proteins. The plastid transit peptide can be recombinantly fused to a second protein in one of several ways. For example, a restriction endonuclease recognition site can be introduced into the nucleotide sequence of the transit peptide at a position corresponding to its C-terminus, and the same or a compatible site can be introduced into the N-terminus of the nucleotide sequence of the target protein.Care must be taken in designing these sites to ensure that the coding sequences of the transit peptide and the second protein remain "in frame" to allow the synthesis of the desired fusion protein. In some cases, it may be preferable to remove the methionine start codon from the second protein when introducing the new restriction site. The introduction of restriction endonuclease recognition sites into both parental molecules and their subsequent joining via recombinant DNA techniques may result in the addition of one or more extra amino acids between the transit peptide and the second protein. Generally, this does not affect targeting activity as long as the cleavage site of the transit peptide remains accessible and functional. The second protein is not altered by the addition of these extra amino acids at its N-terminus. Alternatively, a skilled person can create a precise cleavage site between the transit peptide and the second protein (with or without its initiator methionine) using gene synthesis (Stemmer, et al., (1995) Gene 164:49-53) or similar methods. Furthermore, the fusion of the transit peptide can intentionally include amino acids downstream of the cleavage site. The amino acids at the N-terminus of the mature protein can affect the transit peptide's ability to direct proteins to plastids and / or the efficiency of cleavage after protein import. This may depend on the protein being directed. See, p. e.g., Comai, et al., (1988) J. Biol. Chem. 263(29):15104-9. In some forms, fusion proteins are provided comprising a PIP-72 polypeptide and an insecticidal polypeptide linked by an amino acid connector. It is recognized that DNA sequences can be altered by various methods, and that these alterations can result in DNA sequences encoding proteins with amino acid sequences different from those encoded by the wild-type (or native) pesticide protein. In some forms, a PIP-72 polypeptide can be altered in various ways, including substitutions, deletions, truncations, and insertions of one or more amino acids, including up to 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45 or more substitutions, deletions and / or insertions of amino acids or combinations thereof compared to the polypeptide sequences described in the present description. The methods for such manipulations are generally known in the field. For example, variants of the amino acid sequences of a PIP-72 polypeptide can be prepared by DNA mutations. This can also be accomplished through one of several forms of mutagenesis and / or directed evolution. In some respects, the encoded changes in the amino acid sequence will not substantially affect the protein's function. Such variants will have the desired pesticidal activity. However, it is understood that the ability of a PIP-72 polypeptide to confer pesticidal activity can be enhanced by using such techniques in the compositions described herein. For example, conservative amino acid substitutions can occur in one or more predicted non-essential amino acid residues. A “non-essential” amino acid residue is one that can be altered from the wild-type sequence of a PIP-72 polypeptide without altering its biological activity. A “conservative amino acid substitution” is one in which the amino acid residue is replaced with an amino acid residue that has a similar side chain. Families of amino acid residues with similar side chains have been defined in the material. These families include: amino acids with basic side chains (e.g., lysine, arginine, histidine); acidic side chains (e.g., aspartic acid, glutamic acid); Polar residues with negative charge and their amides (e.g., aspartic acid, asparagine, glutamic acid, glutamine); polar side chains without charge (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine); small aliphatic, nonpolar, or slightly polar residues (e.g., alanine, serine, threonine, proline, glycine); nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan); large, nonpolar aliphatic residues (e.g., methionine, leucine, isoleucine, valine, cysteine); beta-branched side chains (e.g., threonine, valine, isoleucine); aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine); large aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan). Amino acid substitutions can occur in non-conserved regions that retain function. Generally, such substitutions will not occur for conserved amino acid residues or for amino acid residues residing within a conserved motif, where these residues are essential for protein activity. Examples of residues that are conserved and may be essential for protein activity include, for example, residues that are identical among all proteins contained in an alignment of similar or related toxin sequences (e.g., residues that are identical in a homologous alignment). Residues that are conserved but can allow conservative amino acid substitutions while still retaining activity include, for example, residues that have only conservative substitutions among all proteins contained in an alignment of similar or related toxin sequences (e.g., residues that have only conservative substitutions among all proteins contained in the homolog alignment). However, a person skilled in the art will understand that functional variants may have minor conserved or non-conserved alterations in conserved residues. A general guideline of suitable amino acid substitutions that do not affect the biological activity of the protein of interest can be found in the model by Dayhoff et al. (1978) Atlas of Protein Sequence and Structure (Natl. Biomed. Res. Found., Washington, DC), which is incorporated herein by reference. In carrying out these changes, the hydropathic index of the amino acids must be considered. The importance of the hydropathic index of amino acids in conferring interactive biological function in a protein is generally understood in the field (Kyte and Doolittle, (1982) J Mol Biol. 157(1):105-32). It is accepted that the relative hydropathic character of the amino acid contributes to the secondary structure of the resulting protein, which in turn defines the interaction of the protein with other molecules, for example, enzymes, substrates, receptors, DNA, antibodies, antigens, and the like. It is known in the field that certain amino acids can be substituted by other amino acids that have a similar hydropathic index or score and still result in a protein with similar biological activity; that is, a protein with equivalent biological function is still obtained. Each amino acid has been assigned a hydropathic index based on its hydrophobicity and charge characteristics (Kyte and Doolittle, ibid). These are: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine ​​(+2.5); methionine (+1.9); alanine (+1.8); glycine (-0.4); threonine (-0.7); serine (-0.8); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (-3.5); glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9) and arginine (-4.5).In carrying out these changes, the substitution of amino acids whose hydrophilic indices are within +2 is preferred, those within +1 are particularly preferred, and those within +0.5 are preferred even more particularly. It is also understood in this field that the substitution of similar amino acids can be effectively carried out on the basis of hydrophilicity. U.S. Patent No. 4,554,101 describes how the greater average hydrophilicity of a protein, governed by the hydrophilicity of its adjacent amino acids, correlates with a biological property of the protein. As described in U.S. patent accession no. 4,554,101, the following hydrophilicity values ​​have been assigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0, +0.1); glutamate (+3.0.+0.1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (-0.4); proline (-0.5.+0.1); alanine (-0.5); histidine (-0.5); cistena (-1.0); methionine (-1.3); valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3); phenylalanine (-2.5); tryptophan (-3.4). Alternatively, alterations in the protein sequence of many proteins can occur at the amino or carboxyl termini without substantially affecting activity. This can include insertions, deletions, or alterations introduced by modern molecular methods, such as PCR, including PCR amplifications that alter or extend the protein coding sequence by including amino acid-coding sequences in the oligonucleotides used in PCR amplification. Alternatively, the added protein sequences can include sequences coding for entire proteins, such as those commonly used in the field to generate fusion proteins.Such fusion proteins are frequently used to (1) increase the expression of a protein of interest; (2) introduce a binding domain, enzymatic activity, or epitope to facilitate protein purification, protein detection, or other known experimental uses in the field; (3) direct the secretion or translation of a protein to a subcellular organelle, such as the periplasmic space of gram-negative bacteria, mitochondria or chloroplasts of plants, or the endoplasmic reticulum of cells. eukaryotes, the latter of which frequently leads to glycosylation of the protein. The nucleotide and amino acid sequence variants described also include sequences derived from mutagenic and recombinogenic procedures such as DNA shuffling. With this procedure, one or more different PIP-72 polypeptide coding regions can be used to create a novel PIP-72 polypeptide with the desired properties. In this way, recombinant polynucleotide libraries are generated from a population of related polynucleotide sequences comprising sequence regions with substantial sequence identity that can be homologously recombined in vitro or in vivo. For example, using this approach, sequence motifs encoding a domain of interest can be transposed between a pesticide gene and other known pesticide genes to obtain a novel gene encoding a protein with an enhanced property of interest, such as increased insecticidal activity.Strategies for such DNA shuffling are known in the field. See, for example, Stemmer, (1994) Proc. Natl. Acad. Sci. USA 91:10747-10751; Stemmer, (1994) Nature 370:389-391; Crameri, et al., (1997) Nature Biotech. 15:436-438; Moore, et al., (1997) J. Mol. Biol. 272:336-347; Zhang, et al., (1997) Proc. Natl. Acad. Sci. USA 94:4504-4509; Crameri, et al., (1998) Nature 391:288-291; and U.S. patents 5,605,793 and 5,837,458. Domain swapping, or shuffling, is another mechanism for producing altered PIP-72 polypeptides. Domains can be exchanged between PIP-72 polypeptides, resulting in hybrid or chimeric toxins with enhanced insecticidal activity or a broader target spectrum. Methods for generating recombinant proteins and evaluating their pesticidal activity are well known in the field (see, for example, Naimov, et al., (2001) Appl. Environ. Microbiol. 67:5328-5330; de Maagd, et al., (1996) Appl. Environ. Microbiol. 62:1537-1543; Ge, et al., (1991) J. Biol. Chem. 266:17954-17958; Schnepf, et al., (1990) J. Biol. Chem. 265:20923-20930; Rang, et al., (1999) Appl. Environ. Microbiol. 65:2918-2925). Both DNA shuffling and site-directed mutagenesis were used to define polypeptide sequences with pesticidal activity. DNA shuffling was used to generate a recombination-active variant library from the diversity present in GBP_A3175 (20 sequences) and PIP-72Da (10 sequences). A person with expertise in this area can use comparisons with other proteins or functional assays to further define the motifs. High-productivity assessment can be used to evaluate variations of these motifs to determine the function of specific residues. Once these are determined for various motifs, the requirements for a functional protein can be defined. Knowledge of the motifs allows an experienced technician to design sequence variations that will not impact function. The alignment of PIP-72 homologs allowed the identification of residues that are conserved among homologs in this family. Saturation mutagenesis was used to make and test substitutions at selected amino acid positions. These mutants were tested for activity, and a number of active substitutions not present among homologs were identified, providing an understanding of the functional limitations at these residues. Silencers Silencing elements are provided, which, when ingested by the pest, decrease the expression of one or more of the target sequences and thus control the pest (e.g., with insecticidal activity). A “silencing element” is understood to be a polynucleotide that, when it comes into contact with or is ingested by a plant insect pest, is capable of reducing or eliminating the level or expression of a target polynucleotide or the polypeptide it encodes. A silencing element may include a polynucleotide that encodes the polynucleotide that, when it comes into contact with or is ingested by a pest, is capable of reducing or eliminating the level or expression of a target polynucleotide or the polypeptide it encodes. Accordingly, “silencing element,” as used herein, shall be understood to comprise polynucleotides such as RNA constructs, DNA constructs encoding RNA constructs, and expression constructs that These comprise DNA constructs. In one embodiment, the silencing element used can reduce or eliminate the expression level of the target sequence by affecting the level of transcription of the target RNA or, alternatively, by affecting translation and thus the level of the encoded polypeptide. Methods for determining functional silencing elements capable of reducing or eliminating the level of a sequence of interest are described in another section of the present invention. A single polynucleotide used in the described methods may comprise one or more silencing elements for the same or different polynucleotides. The silencing element may be produced in vivo (i.e., in a host cell, such as a plant or microorganism) or in vitro.It shall be understood that “silencing element”, as used in the present description, is used in a manner that includes polynucleotides such as RNA constructs, DNA constructs that encode RNA constructs and / or expression constructs that comprise DNA constructs. As used in this description, a “target sequence” or “target polynucleotide” comprises any sequence in the pest whose expression level is to be reduced. In specific cases, reducing the level of the target sequence in the pest controls the pest. For example, the target sequence may be essential for growth and development. As exemplified elsewhere in this description, reducing the expression level of One or more of these target sequences in a Coleoptera plant pest or a Diabrotica plant pest controls the pest. In some embodiments, a target polynucleotide comprises sequences with ID numbers: 981, 992, 993, 994, or 995. In specific embodiments, a silencing element may comprise a chimeric construct molecule consisting of two or more described sequences. For example, the chimeric construct may be a hairpin or dsRNA, as described herein. A chimera may comprise two or more described sequences. In one embodiment, a chimera comprises two complementary sequences described herein that have some degree of mismatch between the complementary sequences, such that the two sequences are not perfect complements to each other. Supplying at least two different sequences in a single silencing element may allow it to be targeted to multiple genes using a silencing element and / or, for example, an expression cassette. Targeting multiple genes may allow the development of resistance in pests to be slowed or reduced.Additionally, providing multi-targeting capability in an expressed molecule can reduce the expression burden of the plant or transformed plant product, or provide topical treatments that can be targeted to multiple hosts with one application. In specific modalities, the target sequence is not endogenous to the plant. In other modalities, although the silencing element controls pests, preferably, the silencing element has no effect on the normal plant or part of the plant. As described in more detail, silencing elements may include, but are not limited to, a coding suppressor element, a non-coding suppressor element, a double-stranded RNA, a siRNA, an miRNA, or a hairpin suppressor element. The silencing element may further comprise additional sequences that favorably affect the transcription and / or stability of a resulting transcript. For example, silencing elements may comprise at least one thymine residue at the 3' end. This may aid in stabilization. Accordingly, silencing elements may have at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, or more thymine residues at the 3' end. As described in detail below, reducing enhancers may also be used in conjunction with the silencing elements described in the present invention. In one modality, the silencing elements may comprise a chimera, where two or more described sequences, fragments, or active variants, or complements thereof, are found in the same RNA molecule. In several modalities, a described sequence, fragment, or active variant, or complement thereof, may be present as more than one copy in a DNA construct, silencing element, DNA molecule, or RNA molecule. In a hairpin or dsRNA molecule, the location of a sense or antisense sequence in the molecule, for example, where the sequence is transcribed first or is located at a particular end of the RNA molecule, is not limiting of the sequences described, and the dsRNA is not limited by the descriptions in the present description of a particular location for such a sequence. By “reduces” or “that reduces” the expression level of a polynucleotide or polypeptide so encoded, it is meant that the polynucleotide or polypeptide level of the target sequence is statistically lower than the polynucleotide or polypeptide level of the same target sequence in a suitable control pest that is not exposed to (i.e., has not ingested) the silencing element. In particular embodiments of the invention, the reduction of the polynucleotide and / or polypeptide level of the target sequence in a pest according to the present invention results in less than 95%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, less than 10%, or less than 5% of the polynucleotide or polypeptide level of the same target sequence in a suitable control pest. i. Encoding suppression elements As used herein, a “coding suppressor” comprises a polynucleotide designed to express an RNA molecule corresponding to at least a portion of a target messenger RNA in the “coding” orientation. Expression of the RNA molecule comprising the coding suppressor reduces or eliminates the level of the target polynucleotide or the encoded polypeptide in this manner. The polynucleotide comprising the coding suppressor may correspond to all or part of the target polynucleotide sequence, all or part of the 5’ and / or 3’ untranslated region of the target polynucleotide, all or part of the coding sequence of the target polynucleotide, or all or part of both the coding sequence and the untranslated regions of the target polynucleotide. Typically, a coding deletion element has substantial sequence identity with the target polynucleotide, typically greater than approximately 65% ​​sequence identity, greater than approximately 85% sequence identity, or approximately 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity. See U.S. Patent Nos. 5,283,184 and 5,034,323, which are incorporated herein by reference. The coding deletion element may be of any length, as long as it permits deletion of the target sequence. The coding suppression element can be, for example, 15, 16, 17, 18, 19, 20, 22, 25, 30, 50, 100, 150, 200, 250, 300, 350, 400, 450, 500, 600, 700, 900, 1000, 1100, 1200, 1300 nucleotides, or the longest of the target polynucleotides. In other modalities, the coding suppression element may be, for example, approximately 15-25, 19-35, 19-50, 25-100, 100-150, 150-200, 200-250, 250-300, 300-350, 350-400, 450-500, 500-550, 550-600, 600-650, 650-700, 700-750, 750-800, 800-850, 850-900, 900-950, 950-1000, 1000-1050, 1050-1100, 1100-1200, 1200-1300, 1300-1400, 1400-1500, 1500-1600, 1600-1700, 1700-1800 nucleotides or the longest of the target polynucleotides. ii. Non-coding suppression elements As used herein, a “non-coding deletion element” comprises a polynucleotide designed to express an RNA molecule complementary to all or part of a target messenger RNA. Expression of the non-coding deletion element reduces or eliminates the level of the target polynucleotide. The polynucleotide used in the non-coding deletion may correspond to all or part of the complement of the coding sequence of the target polynucleotide, all or part of the complement of the 5' and / or 3' untranslated region of the target polynucleotide, all or part of the complement of the coding sequence of the target polynucleotide, or all or part of the complement of both the coding sequence and the untranslated regions of the target polynucleotide. Additionally, the non-coding deletion element may be completely complementary (i.e., 100% identical) to the complement of the sequence.The non-coding suppressor element may be complementary (i.e., less than 100% identical to the complement of the target sequence) to the target polynucleotide. In specific embodiments, the non-coding suppressor element comprises at least 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence complementarity with the target polynucleotide. Non-coding suppression can be used to inhibit the expression of multiple proteins in the same plant. See, for example, U.S. Patent No. 5,942,657. Furthermore, the non-coding suppressor element may be complementary to a portion of the target polynucleotide. Generally, it is possible to use sequences of at least 15, 16, 17, 18, 19, 20, 22, 25, 50, 100, 200, 300, 400, 450 nucleotides or more of the sequence described in any of the target polynucleotides.Methods for using non-coding suppression to inhibit the expression of endogenous genes in plants are described, for example, in Liu et al. (2002) Plant Physiol. 129:1732-1743 and U.S. Patent Nos. 5,759,829 and 5,942,657, each of which is incorporated in the present invention by reference. iii. Double-stranded RNA deletion element A “double-stranded RNA silencing element” or “dsRNA” comprises at least one transcript that can form a dsRNA either before or after being ingested by a pest. Therefore, a “dsRNA silencing element” includes a dsRNA, a transcript or polyribonucleotide with the capacity to form a dsRNA, or more than one transcript or polyribonucleotide. polyribonucleotide with the ability to form a dsRNA. “Double-stranded RNA” or “bcRNA” refers to a polyribonucleotide structure formed either by a A single self-complementary RNA molecule, or a polyribonucleotide structure formed by the expression of at least two distinct RNA strands. The dsRNA molecule(s) used in the methods and compositions of the invention mediate the reduction of the expression of a target sequence, for example, by mediating RNA interference (RNAi) or gene silencing in a specific form of the sequence. In the context of the present invention, the dsRNA has the ability to reduce or eliminate the level or expression of at least one target polynucleotide or the polypeptide so encoded in a pest. dsRNA can reduce or eliminate the expression level of the target sequence by affecting the level of target RNA transcription, by affecting translation and thus affecting the level of the encoded polypeptide, or by affecting expression at the pretranscriptional level (e.g., by modulating chromatin structure, methylation pattern, etc., to alter gene expression). See, for example, Verdel et al. (2004) Science 303:672-676; Pal-Bhadra et al. (2004) Science 303:669-672; Allshire (2002) Science 297:1818-1819; Volpe et al. (2002) Science 297:1833-1837; Jenuwein (2002) Science 297:2215-2218; and Hall et al. (2002) Science 297:2232-2237. Methods for determining functional dsRNA that has the ability to reduce or eliminate the level of a sequence of interest are described elsewhere section of the present invention. Accordingly, as used in the present description, the term “bcRNA” is intended to encompass other terms used to describe nucleic acid molecules that have the ability to mediate RNA interference or gene silencing, including, for example, small interfering RNA (ipRNA), double-stranded RNA (bcRNA), microRNA (miRNA), hairpin RNA, short hairpin RNA (hcRNA), post-transcriptional gene silencing RNA (sgptRNA), and others. In specific modalities, at least one strand of the double-stranded or duplex region of the dsRNA shares sufficient sequence identity or sequence complementarity with the target polynucleotide to allow the dsRNA to reduce the expression level of the target sequence. As used in the present description, the strand complementary to the target polynucleotide is the “non-coding strand” and the strand homologous to the target polynucleotide is the “coding strand.” In another embodiment, the dsRNA comprises a hairpin RNA. A hairpin RNA comprises an RNA molecule that has the ability to fold back on itself to form a double-stranded structure. Multiple structures can be used as hairpin elements. In specific embodiments, the dsRNA deletion element comprises a hairpin element comprising, in the following order, a first segment, a second segment, and a third segment, where the first and third segments share sufficient complementarity to allow the transcribed RNA to form a double-stranded stem-loop structure. The “second segment” of the hairpin comprises a “loop” or “loop region.” These terms are used interchangeably in this description and should be broadly interpreted to encompass any nucleotide sequence that confers sufficient flexibility to allow self-pairing between complementary regions of a polynucleotide (i.e., segments 1 and 3 that form the stem of the hairpin). For example, in some embodiments, the loop region may be substantially double-stranded and act as a separator between the self-complementary regions of the stem-loop hairpin. In some embodiments, the loop region may comprise a random or non-coding nucleotide sequence and, therefore, does not share sequence identity with a target polynucleotide. In other embodiments, the loop region comprises a coding or non-coding RNA, or a fragment thereof, that shares identity with a target polynucleotide.See, for example, International Patent No. WO 02 / 00904, incorporated herein by reference. In specific embodiments, the loop region can be optimized to be as short as possible while still providing intramolecular flexibility to allow the formation of the stem region with base pairs. Consequently, the loop sequence generally has fewer than 1000, 900, 800, 700, 600, 500, 400, 300, 200, 100, 50, 25, 20, 19, 18, 17, 16, 15, or 10 nucleotides. The “first” and “third” segments of the hairpin RNA molecule comprise the base-paired stem of the hairpin structure. The first and third segments are inverted repeats of each other and share sufficient complementarity to allow the formation of the base-paired stem region. In specific modalities, the first and third segments are fully complementary to each other. Alternatively, the first and third segments may be partially complementary to each other, provided they have the capacity to hybridize to form a base-paired stem region. The amount of complementarity between the first and third segments can be calculated as a percentage of the full segment.Therefore, the first and third hairpin RNA segments generally share at least 50%, 60%, 70%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, up to and even 100% complementarity. The first and third segments are at least approximately 1000, 500, 475, 450, 425, 400, 375, 350, 325, 300, 250, 225, 200, 175, 150, 125, 100, 75, 60, 50, 40, 30, 25, 22, 20, 19, 18, 17, 16, 15, or 10 nucleotides long. In specific forms, the length of the first and / or third segment is approximately 10–100 nucleotides, approximately 10–75 nucleotides, approximately 10–50 nucleotides, or approximately 10–100 nucleotides. approximately 40 nucleotides, from approximately 10 to approximately 35 nucleotides, from approximately 10 to approximately 30 nucleotides, from approximately 10 to approximately 25 nucleotides, from approximately 10 to approximately 19 nucleotides, from approximately 10 to approximately 20 nucleotides, from approximately 19 to approximately 50 nucleotides, from approximately 50 nucleotides to approximately 100 nucleotides, of approximately 100 nucleotides approximately 150 nucleotides, of approximately 100 nucleotides approximately 300 nucleotides, of approximately 150 nucleotides approximately 200 nucleotides, of approximately 200 nucleotides approximately 250 nucleotides, of approximately 250 nucleotides approximately 300 nucleotides, of approximately 300 nucleotides approximately 350 nucleotides, of approximately 350 nucleotides approximately 400 nucleotides, of approximately 400 nucleotides approximately 500 nucleotides, of approximately 600 nt, approximately 700 nt, approximately 800 nt, approximately 900 nt, approximately 1000 nt, approximately 1100 nt, approximately 1200 nt, 1300 nt, 1400 nt, 1500 nt, 1600 nt, 1700 nt, 1800 nt, 1900 nt, 2000 nt or more. In other embodiments, the length of the first and / or third segment comprises at least 10-19 nucleotides, 10-20 nucleotides; 19-35 nucleotides, 20-35 nucleotides; 30-45 nucleotides; 40-50 nucleotides; 50-100 nucleotides; 100-300 nucleotides; approximately 500-700 nucleotides; approximately 700-900 nucleotides; approximately 900-1100 nucleotides; approximately 1300-1500 nucleotides; approximately 1500–1700 nucleotides; approximately 1700–1900 nucleotides; approximately 1900–2100 nucleotides; approximately 2100–2300 nucleotides; or approximately 2300–2500 nucleotides. See, for example, the publication of International Application No. WO02 / 00904. In specific embodiments, the first and third segments comprise at least 20 nucleotides with at least 85% complementarity to the first segment. In other additional embodiments, the first and third segments forming the hairpin stem-loop structure comprise the 3' or 5' overhanging regions with non-matching nucleotide residues. The described hairpin molecules, or double-stranded RNA molecules, can have more than one target sequence, active fragment, or variant, or complements thereof, found in the same portion of the RNA molecule. For example, in a chimeric hairpin structure, the first segment of a hairpin molecule comprises two polynucleotide sections, each with a different target sequence. For example, reading from one end of the hairpin, the first segment is composed of sequences from two separate genes (A followed by B). This first segment is followed by the second segment, the loop portion of the hairpin. The loop segment is followed by the third segment, where the complementary strands to the sequences in the first segment are found (B* followed by A*). By forming the stem-loop hairpin structure, The stem contains Sec. AA* at the distal end of the stem and Sec. BB* proximal to the loop region.In specific modalities, the sequences used in the first, second, and / or third segments comprise domains designed to have sufficient sequence identity with a target polynucleotide of interest and, thus, have the ability to decrease the expression level of the target polynucleotide. Therefore, the specificity of inhibitory RNA transcripts is generally conferred by these silencing element domains.Accordingly, in some embodiments, the first, second, and / or third segment of the silencing element comprises a domain having at least 10, at least 15, at least 19, at least 20, at least 21, at least 22, at least 23, at least 24, at least 25, at least 30, at least 40, at least 50, at least 100, at least 200, at least 300, at least 500, at least 1000, or more than 1000 nucleotides that share sufficient sequence identity with the target polynucleotide to allow a decrease in the expression levels of the target polynucleotide when expressed in a suitable cell.In other forms, the domain is between approximately 15 to 50 nucleotides, approximately 19-35 nucleotides, approximately 20-35 nucleotides, approximately 25-50 nucleotides, approximately 19 to 75 nucleotides, approximately 20 to 75 nucleotides, approximately 40-90 nucleotides, approximately 15-100 nucleotides, 10-100 nucleotides, approximately 10 to approximately 75 nucleotides, approximately 10. to about 50 nucleotides, about 10 to about 40 nucleotides, about 10 to about 35 nucleotides, about 10 to about 30 nucleotides, about 10 to about 25 nucleotides, about 10 to about 20 nucleotides, about 10 to about 19 nucleotides, approximately 50 nucleotides to approximately 100 nucleotides, approximately 100 nucleotides the approximately 150 nucleotides, approximately 150 nucleotides the approximately 200 nucleotides, approximately 200 nucleotides the approximately 250 nucleotides, approximately 250 nucleotides the approximately 300 nucleotides, approximately 300 nucleotides the approximately 350 nucleotides, approximately 350 nucleotides the approximately 400 nucleotides, approximately 400 nucleotides the approximately 500 nucleotides greater. In other forms, the length of the first segment and / or the third segment comprises at least 10-20 nucleotides, at least 10-19 nucleotides, 20-35 nucleotides, 30-45 nucleotides, 40-50 nucleotides, 50-100 nucleotides or approximately 100-300 nucleotides. In specific modalities, the domain of the first, second, and / or third segment has 100% sequence identity with the target polynucleotide. In other modalities, the domain of the first, second, and / or third segment that has homology with the target polypeptide has at least 50%, 60%, 70%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, or 97% homology with the target polypeptide. 98%, 99%, or greater sequence identity with a region of the target polynucleotide. The sequence identity of the domains of the first, second, and / or third segments with the target polynucleotide must be sufficient to reduce the expression of the target polynucleotide of interest. See, for example, Chuang and Meyerowitz (2000) Proc. Natl. Acad. Sci. USA 97:4985-4990; Stoutjesdijk et al. (2002) Plant Physiol. 129:1723-1731; Waterhouse and Helliwell (2003) Nat. Rev. Genet. 04:29-38; Pandolfini et al. BMC Biotechnology 3:7; and U.S. Patent Publication No. 20030175965, which are incorporated herein by reference. A transient assay to determine the effectiveness of hpRNA constructs in silencing gene expression in vivo has been described by Panstruga et al. (2003) Mol. Biol. Rep. 30:135-140. The amount of shared complementarity between the first, second, and / or third segments and the target polynucleotide, or the amount of shared complementarity between the first and third segments (e.g., the stem of the hairpin structure), can vary depending on the organism in which gene expression control is desired. Some organisms or cell types may require an exact match or 100% identity, while other organisms or cell types may tolerate some non-match. In some cells, for example, a single nucleotide non-match in the target sequence negates the ability to suppress gene expression. In these cells, the suppression cassettes described can be used to target gene suppression. Mutants, for example, oncogenes whose transcripts comprise point mutations and can therefore be specifically targeted using the methods and compositions described herein without altering the expression of the remaining wild-type allele. In other organisms, holistic sequence variability can be tolerated as long as some 22-nucleotide region of the sequence is represented with 100% homology between the target polynucleotide and the deletion cassette. In other modalities, the silencing element may comprise a small RNA (pRNA). pRNAs may comprise microRNAs (miRNAs) and small interfering RNAs (pRNAs) (Meister and Tuschl (2004) Nature 431:343-349 and Bonetta et al. (2004) Nature Methods 1:79-86). miRNAs are regulatory agents comprising approximately 19 to approximately 24 ribonucleotides in length, which are highly effective at inhibiting the expression of target polynucleotides. See, for example, Javier et al. (2003) Nature 425: 257-263, incorporated into this description as a reference. For miRNA interference, the silencing element can be designed to express a dsRNA molecule that forms a hairpin or partially base-paired structure, containing a 19, 20, 21, 22, 23, 24 or 25-nucleotide sequence that is complementary to the target polynucleotide of interest.This miRNA can be synthesized or transcribed as a longer RNA that subsequently binds to produce the active miRNA. Specifically, the. A miRNA may comprise 19 nucleotides of the sequence that has homology with a target polynucleotide in the coding orientation and 19 nucleotides of a corresponding non-coding sequence that is complementary to the coding sequence. The miRNA may be an “artificial miRNA” or an “amiRNA” comprising a miRNA sequence that is synthetically designed to silence a target sequence. The methods and compositions described herein use silencing elements that, upon transcription, form a dsRNA molecule. Consequently, the expressed heterologous polynucleotide does not need to form the dsRNA on its own; instead, it can interact with other sequences in the plant cell or in the pest gut after ingestion to enable dsRNA formation. For example, a chimeric polynucleotide that can selectively silence the target polynucleotide can be generated by expressing a chimeric construct comprising the target sequence for a miRNA or siRNA up to a sequence corresponding to all or part of the gene or genes to be silenced. In this embodiment, the dsRNA is formed when the target for the miRNA or siRNA interacts with the existing miRNA in the cell. Subsequently, the resulting dsRNA can reduce the expression level of the gene or genes to be silenced.See, for example, the publication of U.S. patent application no. 2007-0130653, entitled “Methods and Compositions for Gene Silencing.” The construct can be designed to have a target for an endogenous miRNA, or alternatively, it can be employed in. The construct is a target for a heterologous and / or synthetic miRNA. If a heterologous and / or synthetic miRNA is used, it can be introduced into the cell in the same nucleotide construct as the chimeric polynucleotide or in a separate construct. As described in another section of the present invention, any method can be used to introduce the construct comprising the heterologous miRNA. As used in this description, “controlling a pest” or “controls a pest” refers to any effect on a pest that results from limiting the damage the pest causes. Controlling a pest includes, but is not limited to, eliminating the pest, inhibiting pest development, altering pest fertility or growth so that the pest causes less damage to the plant, decreasing the number of offspring produced, producing less fit pests, producing pests more susceptible to predator attack, or preventing pests from eating the plant. Reducing the expression level of the target polynucleotide or the polypeptide encoded in this way in the pest results in the suppression, control, and / or extermination of the invading pathogenic organism. Reducing the expression level of the target sequence in the pest will reduce disease symptoms, resulting in a challenge to the pathogen, by at least approximately 2% to at least approximately 6%, at least approximately 5% to approximately 50%, at least approximately 10% to approximately 60%, at least approximately 30% to approximately 70%, at least approximately 40% to approximately 80%, or at least approximately 50% to approximately 90% or more. Therefore, the methods of the invention can be used to control pests, particularly the Coleoptera plant pest or a Diabrotica plant pest. The assays that determine pest control are commonly known in the field, as are the methods for determining disease resistance in plants following pathogenic infection. See, for example, U.S. Patent No. 5,614,395, incorporated herein by reference. These techniques include measuring over time the average lesion diameter, pathogenic biomass, and the overall percentage of damaged plant tissue. See, for example, Thomma et al. (1998) Plant Biology 95:15107-15111, incorporated herein by reference. See also Baum et al. (2007) Nature Biotech 11:1322-1326 and patent no. WO 2007 / 035650, which carried out tests of both whole vegetable feeding trials and maize root feeding trials. Both references are incorporated in full into this description as a reference. Compositions Also covered are compositions comprising a PIP-72 polypeptide and a silencing element. In some embodiments, the composition comprises a RyanR target silencing element (sec. with ID No.: 992), HP2 sec. with ID No.: 994), or RPS10 (sec. with ID No.: 995). In one embodiment, the composition comprises a PIP-72 polypeptide and a silencing element, wherein the silencing element comprises any of the sec. with ID No.: 982-991, 993, or sec. with ID No.: 561-572 of U.S. patent application no. US2014 / 0275208 and US2015 / 0257389. One or more of the polynucleotides comprising the silencing element may be provided as an external composition, such as a spray or powder for the plant, plant part, seed, a plant insect pest, or a crop area. It is recognized that the composition may comprise a cell (such as a plant cell or a bacterial cell), wherein a polynucleotide encoding PIP-72 and a silencing element is stably incorporated into the genome and operatively binds to active promoters in the cell. In other embodiments, the compositions comprising PIP-72 and a silencing element are not contained within a cell. In such embodiments, the composition may be applied to an area inhabited by a plant insect pest. In one embodiment, the composition is applied externally to a plant (e.g., by spraying a field or crop area) to protect the plant from the pest.The methods for applying nucleotides in this way are known to those with experience in the subject. The composition of the invention can also be formulated as bait. In the present embodiment, the compositions comprise a food substance or an attractant that improves the acceptance of the composition by the pest. The composition comprising PIP-72 and a silencing element may be formulated in a manner suitable for agriculture and / or in an ecologically acceptable carrier. Such carriers may be any material that the animal, plant, or environment to be treated can tolerate. In addition, the carrier must be of such a nature that the composition remains effective in controlling a plant insect pest. Examples of such carriers include water, saline solution, Ringer's solution, dextrose or other sugar solutions, Hank's solution and other physiologically balanced aqueous saline solutions, phosphate regulator, bicarbonate regulator, and Tris regulator. Additionally, the composition may include compounds that increase the half-life of the composition. Furthermore, various insecticidal formulations can be found in, for example, the publication of U.S. patent applications no.2008 / 0275115, 2008 / 0242174, 2008 / 0027143, 2005 / 0042245 and 2004 / 0127520, which are incorporated in this description as a reference. Nucleotide constructs, expression cassettes, and vectors The use of the term “nucleotide constructs” in this description is not intended to limit the modalities to nucleotide constructs that They comprise DNA. Experts in the field will recognize that nucleotide constructs, particularly polynucleotides and oligonucleotides composed of ribonucleotides and combinations of ribonucleotides and deoxyribonucleotides, can also be used in the methods described herein. The nucleotide constructs, nucleic acids, and nucleotide sequences of the modalities further encompass all complementary forms of such constructs, molecules, and sequences. In addition, the nucleotide constructs, nucleotide molecules, and nucleotide sequences of the modalities encompass all nucleotide constructs, molecules, and sequences that can be used in the methods of the modalities for transforming plants, including, but not limited to, those comprising deoxyribonucleotides, ribonucleotides, and combinations thereof. Such deoxyribonucleotides and ribonucleotides include naturally occurring molecules and synthetic analogues.The constructs of nucleotides, nucleic acids, and nucleotide sequences of the modalities also encompass all forms of nucleotide constructs that include, but are not limited to, single-stranded forms, double-stranded forms, hairpins, stem-and-loop structures, and the like. An additional modality relates to a transformed organism, such as a selected organism from plant and insect cells, bacteria, yeast, baculovirus, protozoa, nematodes, and algae. The transformed organism comprises a DNA molecule of the modalities, an expression cassette comprising the DNA molecule or a vector comprising the expression cassette, which can be stably incorporated into the genome of the transformed organism. The modality sequences are provided in DNA constructs for expression in the organism of interest. The construct will include 5' and 3' regulatory sequences operatively linked to a modality sequence. The term "operatively linked," as used herein, refers to a functional link between a promoter and a second sequence, where the promoter sequence initiates and mediates transcription of the DNA sequence corresponding to the second sequence. Generally, operatively linked means that the nucleic acid sequences being linked are contiguous and are necessary to join two protein-coding regions in the same reading frame. The construct may additionally contain at least one additional gene that is cotransformed within the organism. Alternatively, the additional gene(s) may be provided in multiple DNA constructs. The DNA construct will generally include, in the 5' to 3' transcription direction, a transcriptional and translational initiation region (i.e., a promoter), a DNA sequence of the modalities, and a functional transcriptional and translational termination region (i.e., a termination region) in the host organism. The transcriptional initiation region (i.e., the promoter) may be native, analogous, foreign, or heterologous to the organism. host and / or the modality sequence. Additionally, the promoter may be the natural sequence or, alternatively, a synthetic sequence. The term “foreign,” as used in this description, indicates that the promoter is not found in the native organism into which the promoter is introduced. When the promoter is “foreign” or “heterologous” to the modality sequence, it means that the promoter is not the native or naturally occurring promoter for the operatively joined modality sequence. When the promoter is a native or natural sequence, the expression of the operatively joined sequence is altered compared to the wild-type expression, resulting in an altered phenotype. The polynucleotide encoding the silencing element, or used in specific modalities in the methods and compositions described, may be provided in expression cassettes for expression in a plant or organism of interest. It is recognized that multiple silencing elements may be used, including multiple identical silencing elements, multiple silencing elements targeting different regions of the target sequence, or multiple silencing elements targeting different sequences. In the present embodiment, it is recognized that each silencing element may be contained in a single or separate cassette, DNA construct, or vector. As described, any means of providing the silencing element is considered acceptable. In another embodiment, double-stranded RNA is expressed from a deletion cassette. Such a cassette may comprise two convergent promoters that direct the transcription of an operatively linked silencing element. “Convergent promoters” means promoters that are oriented at either end of the functionally linked silencing element, such that each promoter directs transcription of the silencing element in opposite directions, producing two transcripts. In such embodiments, the convergent promoters allow transcription of both the coding and non-coding strands, thereby enabling the formation of a single-stranded RNA. Such a cassette may also comprise two divergent promoters that drive the transcription of one or more of the operatively linked silencing elements.“Divergent promoters” refers to promoters that are oriented in opposite directions, leading to the transcription of one or more silencing elements in opposite directions. In these embodiments, divergent promoters allow the transcription of both coding and non-coding strands and permit the formation of a single-stranded RNA (scRNA). In these embodiments, divergent promoters also allow the transcription of at least two separate hairpin RNAs. In another embodiment, a cassette comprising two or more silencing elements under the control of two separate promoters in the same orientation is present in a construct. In yet another embodiment, two or more individual cassettes, each comprising at least one silencing element, are present. silencing under the control of a promoter, are present in a construct in the same orientation. In some modalities, the DNA construct may also include a transcriptional enhancer sequence. As used in this description, the term “enhancer” refers to a DNA sequence that can stimulate promoter activity and may be an innate promoter element or a heterologous element inserted to increase the level or tissue specificity of a promoter. In this field, several enhancers are known, including, for example, introns with gene expression-enhancing properties in plants (U.S. patent application publication number 2009 / 0144863, the ubiquitin intron (e.g., ma^z ubiquitin intron 1 (see, for example, NCBI sequence S94464; Christensen and Quail (1996) Transgenic Res. 5:213-218; Christensen et al. (1992) Plant Molecular Biology 18:675-689)), the omega enhancer or the omega prime enhancer (Gallie, et al., (1989) Molecular Biology of RNA ed.Cech (Liss, New York) 237-256 and Gallie, et al., (1987) Gene 60:217-25), the CaMV 35S enhancer (see, e.g., Benfey, et al., (1990) EMBO J. 9:1685-96), the maize AdhI intron (Kyozuka et al. (1991) Mol. Gen Genet. 228:40-48; Kyozuka et al. (1990) Maydica 35:353-357), the enhancers of U.S. patent no. 7,803,992, and the sugarcane bacilliform viral (SCBV) enhancer of WO2013130813 may also be used, in addition to those incorporated by reference. The above list of enhancers of the. Transcription is not exclusive. Any suitable transcription enhancer can be used in the modalities. In some embodiments, a DNA construct comprises polynucleotides encoding the PIP-72 polypeptide and a silencing element. In one embodiment, a DNA construct comprises polynucleotides encoding a PIP-72 polypeptide and a silencing element, wherein the silencing element targets RyanR (sequence ident. no. 992), HP2 (sequence ident. no. 994), or RPS10 (sequence ident. no. 995). In another embodiment, a DNA construct comprises polynucleotides encoding a PIP-72 polypeptide and a silencing element, wherein the silencing element comprises any of sequences ident. no. 982-991, 993, or sequence ident. no. 994. of ident.: 561-572 of the publication of the US patent applications no. US2014 / 0275208 and US2015 / 0257389. The termination region may be native to the transcription initiation region, may be native to the operatively bound DNA sequence of interest, may be native to the host plant, or may be derived from another source (i.e., foreign or heterologous to the promoter, the sequence of interest, the host plant, or any combination thereof). Convenient termination regions are available from the Ti plasmid of A. tumefaciens, such as the octopine synthase and nopaline synthase termination regions. See also Guerineau et al. (1991) Mol. Gen Genet. 262:141-144; Proudfoot (1991) Cell 64:671-674; Sanfacon et al. (1991) Genes Dev 5:141-149; Mogen, et al., (1990) Plant Cell 2:1261-1272; Munroe, et al., (1990) Gene 91:151-158; Ballas, et al., (1989) Nucleic Acids Res. 17:7891-7903 and Joshi, et al., (1987) Nucleic Acid Res. 15:9627-9639. When appropriate, a nucleic acid can be optimized to increase expression in the host organism. Therefore, when the host organism is a plant, synthetic nucleic acids can be synthesized using plant-preferred codons to improve expression. See, for example, Campbell and Gowri, (1990) Plant Physiol. 92:1-11 for information on the use of host-preferred codons. For example, although nucleic acid sequences of the modalities can be expressed in both monocotyledonous and dicotyledonous plant species, the sequences can be modified to account for specific codon preferences and GC content preferences of monocotyledons or dicotyledons, as these preferences have been shown to differ (Murray et al. (1989) Nucleic Acids Res. 17:477-498). Therefore, the preferred codon in ma^z for a particular amino acid can be derived from known gene sequences of ma^z.The use of codons in maize for 28 maize plant genes is described in Table 4 of Murray et al., above. Methods for synthesizing preferred genes in plants are available in the field. See, for example, U.S. patents 5,380,831 and 5,436,391 and Murray et al. (1989) Nucleic Acids Res. 17:477-498, and Liu H et al. Mol Bio Rep 37:677-684, 2010, which are incorporated herein by reference. The table of codon usage for Zea maize can be found at kazusa.or.jp / codon / cgi-bin / showcodon.cgi?species=4577, which can be accessed by using the www prefix. A table of Glycine max codon usage can be found at kazusa.or.jp / codon / cgi-bin / showcodon.cgi?species=3847&aa=1&style=N, which can be accessed by using the www prefix. In some forms, the recombinant nucleic acid molecule that encodes a PIP-72 polypeptide has codons optimized for ma^z. It is known that additional sequence modifications enhance gene expression in a host cell. These include the removal of sequences encoding false polyadenylation signals, exon-intron splice site signals, transposon-like repeats, and other well-characterized sequences that can be detrimental to gene expression. The GC content of the sequence can be adjusted to an average concentration for a host cell, as calculated with reference to known genes expressed in the host cell. The term “host cell,” as used herein, refers to a cell that contains a vector and supports the replication and / or expression of the expression vector. Host cells can be prokaryotic cells such as E. coli, or eukaryotic cells such as yeast, insect, amphibian, or mammalian cells, or monocotyledonous or dicotyledonous plant cells.An example of a host cell. monocotyledon is a host cell of maize. When possible, the sequence is modified to avoid hairpin mRNA secondary structures. Expression cassettes may additionally contain 5' leader sequences. Such leader sequences can act to enhance translation. Translation leader sequences are known in the field and include: picornavirus leader sequences, for example, the EMCV leader sequence (5' non-coding region of encephalomyocarditis) (Elroy-Stein, et al., (1989) Proc. Natl. Acad. Sci. USA 86:6126-6130); potyvirus leaders, for example, TEV (tobacco ethinylestradiol) leader (Gallie, et al., (1995) Gene 165(2):233-238), MDMV (maize dwarf mosaic virus) leader, human immunoglobulin heavy chain binding protein (BiP) (Macejak, et al., (1991) Nature 353:90-94); untranslated leader of alfalfa mosaic virus (AMV RNA 4) envelope protein mRNA (Jobling, et al., (1987) Nature 325:622-625); leader of tobacco mosaic virus (TMV) (Gallie, et al., (1989) in Molecular Biology of RNA, ed. Cech (Liss, New York), pp. 237-256) leader of maize chlorotic mottle virus (MCMV) (Lommel, et al., (1991) Virology 81:382-385). See also Della-Cioppa, et al., (1987) Plant Physiol. 84:965-968. Such constructs may also contain a “signal sequence” or “leader sequence” to facilitate co-translational or post-translational transport of the peptide to certain intracellular structures such as the chloroplast (or other plastid), the endoplasmic reticulum, or the Golgi apparatus. “Signal sequence,” as used herein, refers to a sequence known or suspected to trigger co-translational or post-translational transport of the peptide across the cell membrane. In eukaryotes, this typically involves secretion into the Golgi apparatus, with some resulting glycosylation. Insecticidal bacterial toxins are frequently synthesized as protoxins, which are proteolytically activated in the gut of the target pest (Chang, (1987) Methods Enzymol. 153:507-516). In some modalities, the signal sequence is located within the native sequence or may be derived from a sequence of the modalities. “Leader sequence,” as used herein, refers to any sequence that, when translated, results in an amino acid sequence sufficient to trigger co-translational transport of the peptide chain into a subcellular organelle.Therefore, this includes leader sequences that direct transport and / or glycosylation by way of passage to the endoplasmic reticulum, vacuoles, plastids including chloroplasts, mitochondria, and the like. Nuclear-encoded proteins targeting the thylakoid lumen compartment of the chloroplast have a characteristic bipartite transit peptide, composed of a stroma-directing signal peptide and a lumen-directing signal peptide. The stroma-directing information is in the proximal amino portion of the transit peptide. The lumen-directing signal peptide is in the proximal carboxyl portion of the transit peptide and contains all the information for lumen-directing. Recent research in chloroplast proteomics. Researchers in higher plants have identified numerous luminal proteins encoded in the nucleus (Kieselbach et al. FEBS LETT 480:271-276, 2000; Peltier et al. Plant Cell 12:319-341, 2000; Bricker et al. Biochim. Biophys Acta 1503:350-356, 2001), whose signal peptide directing to the lumen can potentially be used in accordance with the present invention. Approximately 80 Arabidopsis proteins, as well as homologous proteins from spinach and pea, are reported by Kieselbach et al., Photosynthesis Research, 78:249-264, 2003. In particular, Table 2 of this publication, which is incorporated in the description as a reference, describes 85 chloroplast lumen proteins, identified by their registration numbers (see also the US patent application publication 2009 / 09044298).In addition, the recently published preliminary version of the rice genome (Goff et al, Science 296:92-100, 2002) is a suitable source of lumen-directing signal peptide that can be used in accordance with the present description. Suitable chloroplast transit peptides (CTPs) are well known to an expert in the field and include, in addition, chimeric CTPs comprising, but not limited to, an N-terminal domain, a core domain, or a C-terminal domain of a CTP from Oryza sativa 1-deoxy-D-xyulose-5-phosphate synthase, Oryza sativa superoxide dismutase, Oryza sativa soluble starch synthase, Oryza sativa NADP-dependent malic acid enzyme, Oryza sativa phospho-2-dehydro-3-deoxyheptonate aldolase 2, Oryza sativa L-ascorbate peroxidase 5, or phosphoglucan aqua dicinase. Oryza sativa, ssRUBISCO from Zea mays, beta-glucosidase from Zea mays, malate dehydrogenase from Zea mays, thioredoxin type M from Zea mays (U.S. Patent Publication No. 2012 / 0304336). Chloroplast transit peptides from U.S. Patent Publications Nos. US20130205440A1, US20130205441A1 and US20130210114A1. The gene for the PIP-72 polypeptide targeted to the chloroplast can be optimized for expression in the chloroplast to account for the differences in codon usage between the plant nucleus and its organelle. In this way, nucleic acids of interest can be synthesized using codons preferred in chloroplasts. See, for example, U.S. Patent No. 5,380,831, incorporated herein by reference. In preparing the expression cassette, the various DNA fragments can be manipulated to provide DNA sequences in the appropriate orientation and, where applicable, in the correct reading frame. For this purpose, adapters or linkers can be used to join the DNA fragments, or other manipulations can be performed to provide convenient restriction sites, remove superfluous DNA, eliminate restriction sites, or similar actions. These manipulations may involve in vitro mutagenesis, primer repair, restriction, hybridization, and substitutions such as transitions and transversions. A number of promoters may be used in practice. Promoters may be selected based on the desired outcome. Nucleic acids may be combined with constitutive, tissue-preferred, inducible, or other promoters for expression in the host organism. The promoters of the present invention include cis element homologs known to effect gene regulation that show homology with the promoter sequences of the present invention. These cis elements include, but are not limited to, oxygen-responsive cis elements (Cowen et al., J Biol. Chem. 268(36):26904-26910 (1993)), light-regulating elements (Bruce and Quaill, Plant Cell 2 (11):1081-1089 (1990); Bruce et al., EMBO J. 10:3015-3024 (1991); Rocholl et al., Plant Sci. 97:189-198 (1994); Block et al., Proc. Natl. Acad. Sci. USA 87:5387-5391 (1990); Giuliano et al., Proc. Natl. Acad. Sci. USA 85:7089-7093 (1988); Staiger et al., Proc. Natl. Acad. Sci.USA 86:6930-6934 (1989); Izawa et al., Plant Cell 6:1277-1287 (1994); Menkens et al., Trends in Biochemistry 20:506-510 (1995); Foster et al., FASEB J. 8:192200 (1994); Plesse et al., Mol Gen Gene 254:258-266 (1997); Green et al., EMBO J. 6:2543-2549 (1987); Kuhlemeier et al., Ann. Rev Plant Physiol. 38:221-257 (1987); Villain et al., J. Biol. Chem. 271:32593-32598 (1996); Lam et al., Plant Cell 2:857-866 (1990); Gilmartin et al., Plant Cell 2:369-378 (1990); Datta et al., Plant Cell 1:1069-1077 (1989); Gilmartin et al., Plant Cell 2:369-378 (1990); Castresana et al., EMBO J. 7:1929-1936 (1988); Ueda et al., Plant Cell 1:217-227 (1989); Terzaghi et al., Annu. Rev. Plant Physiol. Plant Mol. Biol. 46:445-474 (1995); Green et al., EMBO J. 6:2543-2549 (1987); Villain et al., J. Biol. Chem. 271:32593-32598 (1996); Tjaden et al., Plant Cell 6:107-118 (1994); Tjaden et al., Plant Physiol. 108:1109-1117 (1995); Ngai et al., Plant J. 12:1021-1234 (1997); Bruce et al., EMBO J. 10:3015-3024 (1991); Ngai et al., Plant J. 12:1021-1034 (1997)), gibberellin response elements, (Muller et al., J. Plant Physiol. 145:606-613 (1995); Croissant et al., Plant Science 116:27-35 (1996); Lohmer et al., EMBO J. 10:617-624 (1991); Rogers et al., Plant Cell 4:1443-1451 (1992); 2:369-378 (1990); al., Plant Mol. Biol. 14:655-668 (1990), Gubler et al., Plant Cell 7:1879-1891 (1995)), abscisic acid response elements (Busk et al., Plant Cell 9:2261-2270 (1997); Guiltinan et al., Science 250:267-270 (1990); Shen et al., Plant Cell 7:295-307 (1995); Shen et al., Plant Cell 8:1107-1119 (1996); Seo et al., Plant Mol. Biol. 27:1119-1131 (1995); Marcotte et al., Plant Cell 1:969-976 (1989); Shen et al., Plant Cell 7:295-307 (1995); Iwasaki et al., Mol Gen Genet 247:391-398 (1995); Hattori et al., Genes Dev. 6:609-618 (1992); Thomas et al., Plant Cell 5:1401-1410 (1993)), elements similar to absc^sic acid response elements, (Ellerstrom et al., Plant Mol. Biol. 32:1019-1027 (1996)), auxin response elements (Liu et al., Plant Cell 6:645-657 (1994); Physiol. 115:397-407 (1997); Kosugi et al., Plant J. 7:877-886 (1995); (1993)), a cis element responding to methyl jasmonate treatment (Beaudoin and Rothstein, Plant Mol. Biol. 33:835-846 (1997)), a cis element responding to abscisic acid and stress (Straub et al., Plant Mol. Biol. 26:617-630 (1994)), cis elements responding to ethylene (Itzhaki et al., Proc. Natl. Acad. Sci. USA 91:8925-8929 (1994); Montgomery et al., Proc. Natl. Acad. Sci. USA 90:5939-5943 (1993); Sessa et al., Plant Mol. Biol. 28:145-153 (1995); Shinshi et al., Plant Mol. Biol. 27:923-932 (1995)), cis elements responding to salicylic acid, (Strange et al., Plant J. 11:1315-1324 (1997); Qin et al., Plant Cell 6:863-874 (1994)), a cis element responding to water stress and abscisic acid (Lam et al., J. Biol. Chem. 266:17131-17135 (1991); Thomas et al., Plant Cell 5:1401-1410 (1993); Pla et al., Plant Mol Biol 21:259-266 (1993)), an essential cis element for the specific expression of the M phase (Ito et al., Plant Cell 10:331-341 (1998)), sucrose response elements (Huang et al., Plant Mol. Biol. 14:655-668 (1990); Hwang et al., Plant Mol Biol 36:331-341 (1998); Grierson et al., Plant J. 5:815-826 (1994)), heat shock response elements (Pelham et al., Trends Genet. 1:31-35 (1985)), auxin and / or salicylic acid response elements, and are also reported for light regulation (Lam et al., Proc. Natl. Acad. Sci. USA 86:7890-7897 (1989); Benfey et al., Science 250:959-966 (1990)), elements of response to ethylene and salicylic acid (Ohme-Takagi et al., Plant Mol. Biol. 15:941-946 (1990)), elements of response to wounds and abiotic stress (Loake et al., Proc. Natl. Acad. Sci. USA 89:9230-9234 (1992); Mhiri et al.,. Plant Mol. Biol. 33:257-266 (1997)), antioxidant response elements (Rushmore et al., J. Biol. Chem. 266:11632-11639; Dalton et al., Nucleic Acids Res. 22:5016-5023 (1994)), Sph elements (Suzuki et al., Plant Cell 9:799-807 1997)), inducer response elements (Fukuda et al., Plant Mol. Biol. 34:81-87 (1997); Rushton et al., EMBO J. 15:5690-5700 (1996)), metal response elements (Stuart et al., Nature 317:828-831 (1985); Westin et al., EMBO J. 7:3763-3770 (1988); Thiele et al., Nucleic Acids Res. 20:1183-1191 (1992); Faisst et al., Nucleic Acids Res. 20:3-26 (1992)), low temperature response elements, (Baker et al., Plant Mol. Biol. 24:701-713 (1994); Jiang et al., Plant Mol. Biol. 30:679-684 (1996); Nordin et al., Plant Mol. Biol. 21:641-653 (1993); Zhou et al., J. Biol. Chem. 267:23515-23519 (1992));28:605-617 (1995); Bray EA, Trends in Plant Science 2:48-54 (1997)) limones potenciadores para glutenina, (Colot et al., EMBO J. 6:3559-3564 (1987); Thomas et al., Plant Cell 2:1171-1180 (1990); Kreis et al., Philos. trans. R. Soc. Lond., B314:355-365 (1986)), independent regulatory elements of light, (Lagrange et al., Plant Cell 9:1469-1479 (1997); Villain et al., J. Biol. Chem. 271:32593-32598 (1996)), powerful elements of OCS, (Bouchez et al., EMBO J. 8:4197-4204 (1989); Foley et al., Plant J. 3:669-679 (1993)), Elementos ACGT, (Foster et al., FASEB J. 8:192-200 (1994); Izawa et al., Plant Cell 6:1277-1287 (1994); Izawa et al., J. Mol. Biol. 230:1131-1144 (1993)), Elementos cis negativis en genes. related plastids, (Zhou et al., J. Biol. Chem. 267:23515-23519 (1992); Lagrange et al., Mol. Cell Biol. 13:2614-2622 (1993); Lagrange et al., Plant Cell 9:1469-1479 (1997); Zhou et al., J. Biol. Chem. 267:23515-23519 (1992)), elements of the prolamin box, (Forde et al., Nucleic Acids Res. 13:7327-7339 (1985); Colot et al., EMBO J. 6:3559-3564 (1987); Thomas et al., Plant Cell 2:1171-1180 (1990); Thompson et al., Plant Mol. 15:755-764 (1990); Vicente et al., Proc. Natl. Acad. Sci. USA 94:7685-7690 (1997)), IgM heavy chain gene enhancer elements (Gillies et al., Cell 33:717-728 (1983); Whittier et al., Nucleic Acids Res. 15:2515-2535 (1987)). Examples of promoters include: those described in U.S. Patent No. 6,437,217 (maize RS81 promoter), U.S. Patent No. 5,641,876 (rice actin promoter), U.S. Patent No. 6,426,446 (maize RS324 promoter), U.S. Patent No. 6.429.362 (maize PR-1 promoter), U.S. Patent No. 6,232,526 (maize A3 promoter), U.S. Patent No. 6,177,611 (maize constitutive promoters), U.S. Patents Nos. 5,322,938, 5,352,605, 5,359,142 and 5,530,196 (35S promoter), U.S. Patent No. 6,433,252 (maize L3 oleosin promoter, P-Zm.L3), U.S. Patent No. 6,429,357 (rice actin 1 gene promoter as well as a rice actin 2 intron), U.S. Patent No. 5,837,848 (specific root promoter), U.S. patent no. 6,294,714 (light-inducible promoters), U.S. patent no. 6,140,078 (salt-inducible promoters), U.S. patent no. 6,252,138 (pathogen-inducible promoters), U.S. patent no. 6,175,060 (phosphorus-deficiency-inducible promoters), U.S. patent no. 6,635,806 (gamma coixin promoter, PY.Gcx), U.S. patent application serial no. 09 / 757,089 (maize chloroplast aldolase promoter), and U.S. patent no. 8,772,466 (nuclear factor B transcription factor in maize (NFB2)). Suitable constitutive promoters for use in a plant host cell include, for example, the minimal promoter of the Rsyn7 promoter and other constitutive promoters described in patent no. WO 1999 / 43838 and in U.S. patent no. 6,072,050; the minimal promoter CaMV 35S (Odell, et al., (1985) Nature 313:810-812); rice actin (McElroy, et al., (1990) Plant Cell 2:163-171); ubiquitin (Christensen, et al., (1989) Plant Mol. Biol. 12:619-632 and Christensen, et al., (1992) Plant Mol. Biol. 18:675-689); pEMU (Last, et al., (1991) Theor. Appl. Genet. 81:581-588); MAS (Velten, et al., (1984) EMBO J. 3:2723-2730); ALS promoter (U.S. patent no. 5,659,026) and the like. Other constitutive promoters include, for example, those described in U.S. patents nos. 5,608,149; 5,608,144; 5,604,121; 5,569,597; 5,466,785; 5,399,680; 5,268,463; 5,608,142 and 6,177,611.Suitable constitutive promoters also include promoters that have strong expression in almost all tissues but have little expression in pollen, including, but not limited to: Banana streak virus (Acuminata Yunnan) (BSV(AY)) promoters described in U.S. patent no. 8,338,662; promoters of the virus of. banana streak virus (Acuminata Vietnam) (BSV(AV)) described in U.S. Patent No. 8,350,121; and banana streak virus (Mysore) promoters (BSV(MYS)) described in U.S. Patent No. 8,395,022. Depending on the desired outcome, it may be beneficial to express the gene from an inducible promoter. Wound-inducible promoters are of particular interest for regulating the expression of nucleotide sequences in plants. Such wound-inducible promoters can respond to damage caused by insect feeding and include the potato proteinase inhibitor gene (pin II) (Ryan, (1990) Ann. Rev. Phytopath. 28:425-449; Duan, et al., (1996) Nature Biotechnology 14:494-498); wun1 and wun2, U.S. patent no. 5,428,148; win1 and win2 (Stanford, et al., (1989) Mol. Gen Genet. 215:200-208). systemin (McGurl, et al., (1992) Science 225:1570-1573); WIP1 (Rohmeier, et al., (1993) Plant Mol. Biol. 22:783792; Eckelkamp, ​​et al., (1993) FEBS Letters 323:73-76); MPI gene (Corderok, et al., (1994) Plant J. 6(2):141-150) and the like, incorporated herein by reference. Additionally, pathogen-inducible promoters can be used in the nucleotide methods and constructs of the modalities. Such pathogen-inducible promoters include those of pathogenesis-related proteins (PR proteins), which are induced after infection by a pathogen; e.g., PR proteins, SAR proteins, beta-1,3-glucanase, chitinase, etc. See, for example, Redolfi, et al., (1983) Neth. J. Plant Pathol. 89:245-254; Uknes, et al., (1992) Plant Cell 4: 645-656 and Van Loon, (1985) Plant Mol. Virol. 4:111-116. See also patent no. WO 1999 / 43819, which is incorporated in this description by reference. Of interest are promoters that are expressed locally at or near the site of pathogen infection. See, for example, Marineau et al. (1987) Plant Mol. Biol. 9:335-342; Matton et al. (1989) Molecular Plant-Microbe Interactions 2:325-331; Somsisch et al. (1986) Proc. Natl. Acad. Sci. USA 83:2427-2430; Somsisch et al. (1988) Mol. Gen Genet. 2:93-98; and Yang (1996) Proc. Natl. Acad. Sci. USA 93:14972-14977. See also Chen et al. (1996) Plant J. 10:955-966. Zhang, et al., (1994) Proc. Natl. Acad. Sci. USA 91:2507-2511; Warner, et al., (1993) Plant J. 3:191-201; Siebertz, et al., (1989) Plant Cell 1:961-968; U.S. patent no. 5,750,386 (nematode-inducible) and the references cited therein. Of particular interest is the inducible promoter for the PRms gene of maize, whose expression is induced by the pathogen Fusarium moniliforme (see, for example, Cordero, et al., (1992) Physiol. Mol. Plant Path. 41:189-200). Chemically regulated promoters can be used to modulate gene expression in a plant by applying an exogenous chemical regulator. Depending on the objective, the promoter can be a chemically inducible promoter, in which the application of the chemical induces gene expression, or a chemically repressible promoter, in which the application of the chemical represses gene expression. Chemically inducible promoters are known in the field and include, but are not limited to, the maize In2-2 promoter, which is activated by benzenesulfonamide herbicidal protectants, the maize GST promoter, which is activated by electrophilic hydrophobic compounds used as pre-emergent herbicides, and the tobacco PR-1a promoter, which is activated by salicylic acid. Other chemically regulated promoters that may be of interest include steroid-responsive promoters (see, for example, the glucocorticoid-inducible promoter in Schena, et al., (1991) Proc. Natl. Acad. Sci. USA 88:10421-10425 and McNellis, et al., (1998) Plant J. 14(2):247-257) and tetracycline-inducible and tetracycline-repressible promoters (see, for example, Gatz, et al., (1991) Mol. Gen Genet. 227:229-237 and U.S. patents 5,814,618 and 5,789,156), incorporated herein by reference. Tissue-specific promoters can be used to direct enhanced expression of the PIP-72 polypeptide within a particular plant tissue. Preferred tissue promoters include those described in Yamamoto et al. (1997) Plant J. 12(2):255-265; Kawamata et al. (1997) Plant Cell Physiol. 38(7):792-803; Hansen et al. (1997) Mol. Gen Genet. 254(3):337-343; Russell et al. (1997) Transgenic Res. 6(2):157-168; Rinehart et al. (1996) Plant Physiol. 112(3):1331-1341; Van Camp et al. (1996) Plant Physiol. 112(2):525-535. Canevascini, et al., (1996) Plant Physiol. 112(2):513-524; Yamamoto, et al., (1994) Plant Cell Physiol. 35(5):773-778; Lam, (1994) Results Probl. Cell Differ. 20:181-196; Orozco, et al., (1993) Plant Mol Biol. 23(6):1129-1138; Matsuoka, et al., (1993) Proc Natl. Acad. Sci. USA 90(20):9586-9590 and Guevara-Garcia, et al., (1993) Plant J. 4(3):495-505. Such promoters can be modified, if necessary, for weak expression. Leaf-specific promoters are known in the field. See, for example, Yamamoto, et al., (1997) Plant J. 12(2):255-265; Kwon, et al., (1994) Plant Physiol. 105:357-67; Yamamoto, et al., (1994) Plant Cell Physiol. 35(5):773-778; Gotor, et al., (1993) Plant J. 3:509-18; Orozco, et al., (1993) Plant Mol. Biol. 23(6):1129-1138 and Matsuoka, et al., (1993) Proc. Natl. Acad. Sci. USA 90(20):9586-9590. Preferred root-specific promoters are known and can be selected from the many available in the literature or isolated de novo from several compatible species. See, for example, Hire, et al., (1992) Plant Mol. Biol. 20(2):207-218 (soybean root-specific glutamine synthetase gene); Keller and Baumgartner, (1991) Plant Cell 3(10):1051-1061 (root-specific control element in the green bean GRP 1.8 gene); Sanger, et al., (1990) Plant Mol. Biol. 14(3):433-443 (root-specific promoter of the mannopin synthase (MAS) gene from Agrobacterium tumefaciens) and Miao, et al., (1991) Plant Cell 3(1):11-22 (full-length cDNA clone encoding cytosolic glutamine synthetase (GS), expressed in roots and root nodules of soybean). See also Bogusz, et al., (1990) Plant Cell 2(7):633-641, where two specific promoters are described. Root-specific hemoglobin genes were isolated from the nitrogen-fixing non-legume *Parasponia andersonii* and the related non-legume non-nitrogen-fixing *Trema tomentosa*. The promoters of these genes were joined to a p-glucuronidase reporter gene and introduced into the non-legume *Nicotiana tabacum* and the legume *Lotus corniculatus*, and in both cases, root-specific promoter activity was retained. Leach and Aoyagi (1991) describe their analysis of the promoters of the highly expressed root-inducing genes *rolC* and *rolD* from *Agrobacterium rhizogenes* (see *Plant Science* (Limerick) 79(1):69–76). They concluded that the tissue-preferred enhancer and DNA determinants are dissociated at these promoters. Teeri et al.(1989) used gene fusion to lacZ to demonstrate that the Agrobacterium T-DNA gene encoding octopine synthase is especially active in the root apex epidermis and that the TR2' gene is root-specific in the intact plant and is stimulated by wounds in the leaf tissue, a combination of characteristics especially desirable for use with an insecticidal or larvicidal gene (see, EMBO J. 8(2):343-350). The TR1' gene fused to nptII (neomycin phosphotransferase II) showed similar characteristics. Other preferred promoters in the root include the VfENOD-GRP3 gene promoter (Kuster, et al., (1995) Plant Mol. Biol. 29(4):759-772) and the rolB promoter (Capana, et al., (1994) Plant Mol. Biol. 25(4):681-691). See also U.S. patents Nos. 5,837,876; 5,750,386; 5,633,363; 5,459,252; 5,401,836; 5,110,732 and. 5,023,179. Preferred root regulatory sequences of Arabidopsis thaliana are described in U.S. patent application US20130117883. Preferred root RCc3 promoters of sorghum (Sorghum bicolor) are described in U.S. patent application US20120210463. Preferred root promoters in maize are described in U.S. patent application publication 20030131377, U.S. patent no. 7,645,919, and 8,735,655. Cap-specific root promoters (ZmRCPI) in maize are described in U.S. patent application publication no. 20130025000. The preferred promoters of ra^z in ma^z of the publication of U.S. patent application no. 20130312136. “Preferred seed” promoters include “seed-specific” promoters (those promoters that are active during seed development, such as seed storage protein promoters) as well as “seed germination” promoters (those promoters that are active during seed germination). See Thompson et al. (1989) BioEssays 10:108, which is incorporated herein by reference. Such preferred seed promoters include, but are not limited to, Cim1 (cytokinin-induced messaging); cZ19B1 (maize 19 kDa zeena); and milps (myo-inositol-1-phosphate synthase) (see U.S. Patent No. 6,225,529, incorporated herein by reference). Gamma-zeena and Glb-1 are endosperm-specific promoters. For dicotyledons, seed-specific promoters include, but are not limited to, inhibitor of Kunitz trypsin 3 (KTi3) (Jofuku and Goldberg, (1989) Plant Cell 1:1079-1093), bean phaseolin, napine, O-conglycinin, glycinin 1, soybean lectin, cruciferin, and the like. For monocots, seed-specific promoters include, but are not limited to, maize 15 kDa zein, 22 kDa zein, 27 kDa zein, g-zein, ceros, shrunken 1, shrunken 2, globulin 1, etc. See also patent number WO 2000 / 12733, which describes the preferred seed promoters of the end1 and end2 genes; which are incorporated herein by reference. In dicotyledonous plants, specific seed promoters include, but are not limited to, the Arabidopsis seed coat promoter, pBAN; and the Arabidopsis premature seed promoters, p26, p63 and p63tr (U.S. patents Nos. 7,294,760 and 7,847,153).A promoter that has a "preferred" expression in a particular tissue is expressed in that tissue more than in at least one other plant tissue. Some tissue-preferred promoters show expression almost exclusively in that particular tissue. When a low level of expression is desired, weak promoters are used. Generally, the term “weak promoter,” as used herein, refers to a promoter that directs the expression of a coding sequence at a low level. By low level of expression, we mean levels of approximately 1 / 1000 transcripts to approximately 1 / 100,000 transcripts to approximately 1 / 500,000 transcripts. Alternatively, it is recognized that the term “weak promoters” also encompasses promoters that direct the Expression occurs in only a few cells and not in others, resulting in a low overall level of expression. When a promoter drives expression to unacceptably high levels, portions of the promoter sequence can be deleted or modified to decrease expression levels. Such weak constitutive promoters include, for example, the minimal promoter of the Rsyn7 promoter (patent no. WO 1999 / 43838 and U.S. patent no. 6,072,050), the minimal 35S promoter of CaMV, and the like. Other constitutive promoters include, for example, those described in U.S. patents nos. 5,608,149; 5,608,144; 5,604,121; 5,569,597; 5,466,785; 5,399,680; 5,268,463; 5,608,142 and 6,177,611, which are incorporated herein by reference. The above list of promoters is not exhaustive. Any suitable promoter may be used in the modalities. Generally, the expression cassette will include a selectable marker gene for selecting transformed cells. Selectable marker genes are used for selecting transformed cells and tissues. Marker genes include genes that encode antibiotic resistance, such as those encoding neomycin phosphotransferase II (NEO) and hygromycin phosphotransferase (HPT), as well as genes that confer resistance to herbicide compounds, such as glufosinate ammonium, bromyxinyl, imidazolinones, and 2,4-dichlorophenoxyacetate (2,4-D). Additional examples of selectable marker genes are provided. Suitable genes include, but are not limited to, genes encoding resistance to chloranlenicol (Herrera Estrella, et al., (1983) EMBO J. 2:987-992); methotrexate (Herrera Estrella, et al., (1983) Nature 303:209-213 and Meijer, et al., (1991) Plant Mol. Biol. 16:807-820); streptomycin (Jones, et al., (1987) Mol. Gen Genet. 210:86-91); spectinomycin (Bretagne-Sagnard, et al., (1996) Transgenic Res. 5:131-137); bleomycin (Hille, et al., (1990) Plant Mol. Biol. 7:171-176); sulfonamide (Guerineau, et al., (1990) Plant Mol. Biol. 15:127-136); bromoxynil (Stalker, et al., (1988) Science 242:419-423); glyphosate (Shaw, et al., (1986) Science 233:478-481 and U.S. patent applications serial numbers 10 / 004.357 and 10 / 427.692); phosphinothricin (DeBlock, et al., (1987) EMBO J. 6:2513-2518). See generally, Yarranton, (1992) Curr. Opin. Biotech. 3:506-511; Christopherson, et al., (1992) Proc. Natl. Acad. Sci USA 89:6314-6318; Yao, et al., (1992) Cell 71:63-72; Reznikoff, (1992) Mol.Microbiol. 6:2419-2422; Barkley, et al., (1980) en The Operon, pags. 177-220; Hu, et al., (1987) Cell 48:555-566; Brown, et al., (1987) Cell 49:603-612; Figge, et al., (1988) Cell 52:713-722; Deuschle, et al., (1989) Proc. Natl. Acad. Sci. USA 86:5400-5404; Fuerst, et al., (1989) Proc. Natl. Acad. Sci. USA 86:2549-2553; Deuschle, et al., (1990) Science 248:480-483; Gossen, (1993) Ph.D. Thesis, University of Heidelberg; Reines, et al., (1993) Proc. Natl. Acad. Sci. USA 90:1917-1921; Labow, et al., (1990) Mol. Cell. Biol. 10:3343-3356; Zambretti, et al., (1992) Proc. Natl. Acad. Sci. USA 89:39523956; Baim, et al., (1991) Proc. Natl. Acad. Sci. USA 88:5072-5076; Wyborski,. et al., (1991) Nucleic Acids Res. 19:4647-4653; Hillenand-Wissman, (1989) Topics Mol. Struc. Biol. 10:143-162; Degenkolb, et al., (1991) Antimicrob. Agents Chemother. 35:1591-1595; Kleinschnidt, et al., (1988) Biochemistry 27:1094-1104; Bonin, (1993) Ph.D. Thesis, University of Heidelberg; Gossen, et al., (1992) Proc. Natl. Academic Sci USA 89:5547-5551; Oliva, et al., (1992) Antimicrob. Agents Chemother. 36:913-919; Hlavka, et al., (1985) Handbook of Experimental Pharmacology, Vol. 78 (Springer-Verlag, Berlin) and Gill, et al., (1988) Nature 334:721-724. Such descriptions are incorporated in the present description by reference. The above list of selectable marker genes is not exclusive. Any selectable marker gene can be used in the modalities. Plant transformation The methods described herein involve introducing a polypeptide or polynucleotide into a plant. “Introduce,” as used herein, means presenting the polynucleotide or polypeptide to the plant in such a way that the sequence gains access to the interior of a plant cell. The methods described herein do not depend on a particular method for introducing a polynucleotide or polypeptide into a plant, but only on the polynucleotide or polypeptides gaining access to the interior of at least one plant cell. Methods for introducing polynucleotides or polypeptides into plants are known in the field and include, but are not limited to, methods of stable transformation, transient transformation methods, and virus-mediated methods. “Stable transformation,” as used herein, means that the nucleotide construct introduced into a plant integrates into the plant genome and is capable of being inherited by its progeny. The term “transient transformation,” as used herein, means that a polynucleotide is introduced into a plant and does not integrate into the plant genome, or that a polypeptide is introduced into a plant. The term “plant,” as used herein, refers to whole plants, plant organs (e.g., leaves, stems, roots, etc.), seeds, plant cells, propagules, embryos, and their progeny. Plant cells may be differentiated or undifferentiated (e.g., callus, suspension culture cells, protoplasts, leaf cells, root cells, phloem cells, and pollen). Transformation protocols, as well as protocols for introducing nucleotide sequences into plants, can vary depending on the type of plant or plant cell, i.e., monocotyledons or dicotyledons, intended for transformation. Suitable methods for introducing nucleotide sequences into plant cells and subsequent insertion into the plant genome include microinjection (Crossway, et al., (1986) Biotechniques 4:320-334), electroporation (Riggs, et al., (1986) Proc. Natl. Acad. Sci. USA 83:5602-5606), and Agrobacterium-mediated transformation. (U.S. patents nos. 5,563,055 and 5,981,840), direct gene transfer (Paszkowski, et al., (1984) EMBO J. 3:2717-2722) and ballistic particle acceleration bombardment (see, for example, U.S. patents nos. 4,945,050; 5,879,918; 5,886,244 and 5,932,782; Tomes, et al., (1995) in Plant Cell, Tissue, and Organ Culture: Fundamental Methods, ed. Gamborg and Phillips, (Springer-Verlag, Berlin) and McCabe, et al., (1988) Biotechnology 6:923-926) and Lecl transformation (patent no. WO 00 / 28058). For potato transformation, see Tu, et al., (1998) Plant Molecular Biology 37:829-838 and Chong, et al., (2000) Transgenic Research 9:71-78. Other transformation procedures can be found in Weissinger, et al., (1988) Ann. Rev. Genet. 22:421-477; Sanford, et al., (1987) Particulate Science and Technology 5:27-37 (onion); Christou, et al., (1988) Plant Physiol. 87:671-674 (soybean); McCabe, et al., (1988) Bio / Technology 6:923-926 (soybean); Finer and McMullen, (1991) In Vitro Cell Dev. Biol. 27P:175–182 (soybean); Singh, et al., (1998) Theor. Appl. Genet. 96:319–324 (soybean); Datta, et al., (1990) Biotechnology 8:736-740 (rice); Klein, et al., (1988) Proc. Natl. Sunday. Ski. USA 85:4305-4309 (mafz); Klein, et al., (1988) Biotechnology 6:559-563 (mafz); patents of the EE. YU. man. 5,240,855; 5,322,783 and 5,324,646; Klein, et al., (1988) Plant Physiol. 91:440–444 (mafz); Fromm, et al., (1990) Biotechnology 8:833-839 (ma^z); Hooykaas-Van Slogteren, et al., (1984) Nature (London) 311:763-764; patents of the EE. YU. man. 5,736,369 (cereals); Bytebier, et al., (1987) Proc. Natl. Sunday. Ski. USA 84:5345–5349. (liliaceae); De Wet, et al., (1985) in The Experimental Manipulation of Ovule Tissues, ed. Chapman, et al., (Longman, New York), pags. 197–209 (pollen); Kaeppler, et al., (1990) Plant Cell Reports 9:415-418 y Kaeppler, et al., (1992) Theor. Appl. Genet. 84:560-566 (whisker-mediated transformation); D'Halluin, et al., (1992) Plant Cell 4:1495-1505 (electroporation); Li, et al., (1993) Plant Cell Reports 12:250-255 and Christou y Ford, (1995) Annals of Botany 75:407-413 (rice); Osjoda, et al., (1996) Nature Biotechnology 14:745-750 (ma^za traves de Agrobacterium tumefaciens); all of which are incorporated into this description as reference. In specific modalities, the modality sequences can be delivered to a plant by various transient transformation methods. Such transient transformation methods include, but are not limited to, the introduction of the PIP-72 polypeptide or variants and fragments thereof and a polynucleotide encoding a silencing element directly into the plant, or the introduction of the PIP-72 polypeptide transcript and a silencing element into the plant. Such methods include, for example, microinjections or particle bombardment. See, for example, Crossway et al. (1986) Mol Gen. Genet. 202:179-185; Nomura et al. (1986) Plant Sci. 44:53-58; Hepler et al. (1994) Proc. Natl. Acad. Sci. 91:2176-2180 and Hush, et al., (1994) The Journal of Cell Science 107:775-784, all of which are incorporated into the present description by reference. Alternatively, the PIP-72 polypeptide polynucleotide can be temporarily transformed into The plant is inoculated using known techniques. These techniques include the viral vector system and polynucleotide precipitation in a form that excludes subsequent DNA release. Therefore, transcription of the DNA bound to the particles can occur, but the frequency with which it is released to integrate into the genome is greatly reduced. Such methods include the use of polyethyleneimine-coated particles (PEI; Sigma No. P3143). Methods for the targeted insertion of a polynucleotide into a specific site in the plant genome are known in this field. In one embodiment, the insertion of the polynucleotide into a desired genomic location is achieved through the use of a site-specific recombination system. See, for example, patents WO 1999 / 25821, WO 1999 / 25854, WO 1999 / 25840, WO 1999 / 25855, and WO 1999 / 25853, all of which are incorporated herein by reference. Briefly, the polynucleotide in the embodiments may be contained in a transfer cassette flanked by two non-identical recombination sites. The transfer cassette is introduced into a plant that has a target site stably incorporated into its genome, flanked by two non-identical recombination sites that correspond to the sites on the transfer cassette. An appropriate recombinase is provided, and the transfer cassette integrates into the target site.The polynucleotide of interest is thus integrated into a specific chromosomal position in the plant genome. Plant transformation vectors can consist of one or more DNA vectors necessary to achieve plant transformation. For example, it is common practice in this field to use plant transformation vectors composed of more than one contiguous DNA segment. These vectors are frequently referred to as “binary vectors.” Binary vectors, as well as vectors with auxiliary plasmids, are most often used for Agrobacterium-mediated transformation, where the size and complexity of the DNA segments required for efficient transformation are very large, and it is advantageous to separate the functions into separate DNA molecules.Binary vectors typically contain a plasmid vector that includes the cis-acting sequences required for T-DNA transfer (such as the left and right borders), a selection marker modified to be expressible in a plant cell, and a gene of interest (a gene modified to be expressible in a plant cell from which transgenic plants are desired). This plasmid vector also contains the sequences required for bacterial replication. The cis-acting sequences are arranged to allow efficient transfer to and expression within plant cells. For example, the selectable marker gene and the pesticide gene are located between the left and right borders. A second plasmid vector often contains the trans-acting factors that mediate the transfer of Agrobacterium T-DNA to plant cells. The plasmid frequently contains virulence functions (Vir genes) that enable infection of plant cells by Agrobacterium, and DNA transfer by cleavage at border sequences and Vir-mediated DNA transfer, as discussed in the subject (Hellens and Mullineaux, (2000) Trends in Plant Science 5:446-451). Several types of Agrobacterium strains (e.g., LBA4404, GV3101, EHA101, EHA105, etc.) can be used for plant transformation. The second plasmid vector is not required for plant transformation by other methods such as microprojection, microinjection, electroporation, polyethylene glycol, etc. In general, plant transformation methods involve transferring heterologous DNA into target plant cells (e.g., immature or mature embryos, suspension cultures, undifferentiated callus, protoplasts, etc.), followed by the application of an appropriate maximum threshold level of selection (depending on the selection marker gene) to recover transformed plant cells from a mass of untransformed cells. After integration of the heterologous foreign DNA into the plant cells, an appropriate maximum threshold level of selection is then applied to the medium to eliminate untransformed cells and separate and proliferate any potentially transformed cells that survive this selection treatment by regularly transferring them to fresh medium. Through continuous passages and challenges with appropriate selection, cells transformed with the plasmid vector are identified and proliferated. Subsequently, methods can be used molecular and biochemical tests to confirm the presence of the heterologous gene of interest integrated into the genome of the transgenic plant. The explants are typically transferred to a fresh supply of the same medium and routinely cultured. Subsequently, the transformed cells differentiate into shoots after being placed in regeneration medium supplemented with a maximum threshold level of a selection agent. The shoots are then transferred to a selective rooting medium to recover rooted shoots or plantlets. The transgenic plantlet is then grown into a mature plant and produces fertile seeds (e.g., Hiei et al. (1994) The Plant Journal 6:271-282; Ishida et al. (1996) Nature Biotechnology 14:745-750). A general description of the techniques and methods for generating transgenic plants can be found in Ayres and Park, (1994) Critical Reviews in Plant Science 13:219-239 and Bommineni and Jauhar, (1997) Maydica 42:107-120.Since the transformed material contains various cell types, both transformed and untransformed cells are present in any piece of callus, tissue, or group of cells under consideration. The ability to remove untransformed cells and allow transformed cells to proliferate results in transformed plant cultures. Frequently, the ability to remove untransformed cells is a limitation for this process. rapid recovery of transformed plant cells and successful generation of transgenic plants. The transformed cells can develop into plants according to conventional methods. See, for example, McCormick et al. (1986) Plant Cell Reports 5:81-84. These plants can then be grown and pollinated with the same transformed strain or with different strains, and the resulting hybrid will have the constitutive or inducible expression of the desired identified phenotypic trait. Two or more generations can be grown to ensure that the expression of the desired phenotypic trait is maintained and stably inherited, and then the seeds can be harvested to ensure that the expression of the desired phenotypic trait has been achieved. The nucleotide sequences of the modalities can be provided to the plant by exposing the plant to a virus or viral nucleic acids. Generally, such methods involve incorporating the nucleotide construct of interest within a viral DNA or RNA molecule. It is recognized that recombinant proteins of the modalities can initially be synthesized as part of a viral polyprotein, which can then be processed by proteolysis in vivo or in vitro to produce the desired PIP-72 polypeptide. It is further recognized that such a viral polyprotein, comprising at least a portion of the amino acid sequence of a PIP-72 polypeptide of the modalities, can have pesticidal activity. desired. The methods encompass such viral polyproteins and the nucleotide sequences that encode them. The methods for providing plants with nucleotide constructs and producing the encoded proteins in the plants involve the viral DNA or RNA molecules known in the field. See, for example, U.S. Patent Nos. 5,889,191; 5,889,190; 5,866,785; 5,589,367 and 5,316,931; which are incorporated herein by reference. Methods for chloroplast transformation are known in the field. See, for example, Svab et al. (1990) Proc. Natl. Acad. Sci. USA 87:8526-8530; Svab and Maliga (1993) Proc. Natl. Acad. Sci. USA 90:913-917; Svab and Maliga (1993) EMBO J. 12:601-606. The method is based on delivering DNA containing a selectable marker via a particle gun and directing the DNA to the plasmid genome through homologous recombination. Additionally, plastid transformation can be achieved by transactivating a silent plastid transgene through tissue-preferential expression of a plastid-targeted, nuclear-encoded RNA polymerase. This system has been reported in McBride, et al., (1994) Proc. Natl. Acad. Sci. USA 91:7301-7305. The modalities also refer to the plant propagation material of a transformed plant of the modalities which include, but are not limited to, seeds, tubers, corms, bulbs, leaves and root and shoot cuttings. The methods can be used for the transformation of any plant species, including, but not limited to, monocots and dicots. Examples of plants of interest include, but are not limited to, maize (Zea mays), Brassica sp. (e.g., B. napus, B. rapa, B. juncea), particularly Brassica species useful as sources of seed oil, alfalfa (Medicago sativa), rice (Oryza sativa), rye (Secale cereale), sorghum (Sorghum bicolor, Sorghum vulgare), millet (e.g., pearl millet (Pennisetum glaucum), common millet (Panicum miliaceum), moha (Setaria italica), finger millet (Eleusine coracana)), sunflower (Helianthus annuus), safflower (Carthamus tinctorius), wheat (Triticum aestivum), soybean (Glycine max), tobacco (Nicotiana tabacum), potato (Solanum tuberosum), peanut (Arachis hypogaea), cotton (Gossypium barbadense, Gossypium hirsutum), sweet potato (Ipomoea batatus), cassava (Manihot esculenta), coffee (Coffea spp.), coconut (Cocos nucifera), pineapple (Ananas comosus), citrus trees (Citrus spp.), cacao (Theobroma cacao), tea (Camellia sinensis), banana (Musa spp.), avocado (Persea americana), fig (Ficus casica), guava (Psidium guajava), mango (Mangifera indica), olive (Olea europaea), papaya (Carica papaya), cashew nut (Anacardium occidentale), macadamia (Macadamia integrifolia), almond (Prunus amygdalus), sugar beet (Beta vulgaris), sugar cane (Saccharum spp.), oats, barley, vegetables, ornamental plants, and conifers. Vegetables include tomatoes (Lycopersicon esculentum), lettuce (e.g., Lactuca sativa), green beans (Phaseolus vulgaris), lima beans (Phaseolus limensis) peas (Lathyrus spp.), and members of the genus Cucumis such as cucumber (C. sativus), melon (C. cantaloupensis), and muskmelon (C. melo). Ornamental plants include azalea (Rhododendron spp.), hydrangea (Macrophylla hydrangea), hibiscus (Hibiscus rosasanensis), roses (Rosa spp.), tulip (Tulipa spp.), daffodil (Narcissus spp.), petunia (Petunia hybrida), carnation (Dianthus caryophyllus), poinsettia (Euphorbia pulcherrima), and chrysanthemum.Conifers that can be used in the practice of the modalities include, for example, pines, such as loblolly pine (Pinus taeda), elliottii pine (Pinus elliotii), ponderosa pine (Pinus ponderosa), Murraya pine (Pinus contorta), and Monterey pine (Pinus radiata); Douglas fir (Pseudotsuga menziesii); western hemlock (Tsuga canadensis); Sitka spruce (Picea glauca); coast redwood (Sequoia sempervirens); true firs such as the common fir (Abies amabilis) and balsam fir (Abies balsamea); and cedars, such as western red cedar (Thuja plicata) and Alaskan yellow cedar (Chamaecyparis nootkatensis). The plants in the modalities include crop plants (e.g., maize, alfalfa, sunflower, Brassica, soybean, cotton, safflower, peanut, sorghum, wheat, millet, tobacco, etc.), such as maize and soybean plants. Grasses include, but are not limited to: winter grass (Poa annua); annual ryegrass (Lolium multiflorum); Canada grass (Poa compressa); red fescue (Festuca rubra); common bentgrass (Agrostis tenuis); swamp bentgrass (Agrostis palustris); forage wheat (Agropyron desertorum); crested wheat (Agropyron cristatum); hard fescue (Festuca longifolia); Kentucky bluegrass (Poa pratensis); common fescue (Dactylis glomerata); perennial ryegrass (Lolium perenne); red fescue (Festuca rubra); stonegrass (Agrostis alba); common fescue (Poa trivialis); sheep fescue (Festuca ovina); unarmed brome (Bromus inermis); tall grass (Festuca arundinacea); timothy (Phleum pratense); dog grass (Agrostis canina); weeping alkaline grass (Puccinellia distans); western wheatgrass (Agropyron smithii); Bermuda grass (Cynodon spp.); St. Augustine grass (Stenotaphrum secundatum); zoysia grass (Zoysia spp.); Bahia grass (Paspalum notatum); carpet grass (Axonopus affinis); centipede grass (Eremochloa ophiuroides); kikuyo grass (Pennisetum clandesinum); coastal paspalum (Paspalum vaginatum); navajita azul (Bouteloua slender); buffalo paste (Buchloe dactyloids); pasto banderita (Bouteloua curtipendula). Plants of interest include grain plants that provide seeds of interest, oilseed plants, and legume plants. Seeds of interest include grain seeds such as maize, wheat, barley, rice, sorghum, rye, millet, etc. Oilseed plants include cotton, soybeans, safflower, sunflower, brassicas, maize, alfalfa, palm, coconut, flax, castor bean, olive, etc. Legume plants include beans and peas. Beans include guar, carob, fenugreek, soybeans, kidney beans, mung beans, broad beans, lentils, chickpeas, etc. Evaluation of plant transformation After the introduction of heterologous foreign DNA into plant cells, the transformation or integration of the heterologous gene into the plant genome is confirmed by various methods such as the analysis of nucleic acids, proteins, and metabolites associated with the integrated gene. PCR analysis is a rapid method for analyzing transformed cells, tissues, or shoots for the presence of the incorporated gene at the earliest stage before transplantation into soil (Sambrook and Russell, (2001) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY). PCR is performed using oligonucleotide primers specific to the gene of interest or the Agrobacterium vector background, etc. Plant transformation can be confirmed by Southern blot membrane analysis of genomic DNA (Sambrook and Russell, (2001) above). In general, total DNA is extracted from the transformant, digested with appropriate restriction enzymes, fractionated on an agarose gel, and transferred to a nitrocellulose or nylon membrane. The membrane, or “transfer,” is then tested with, for example, a 32P-labeled target DNA fragment to confirm the integration of the introduced gene into the plant genome according to standard techniques (Sambrook and Russell, (2001) above). In Northern membrane analysis, RNA is isolated from specific tissues of the transformant, fractionated on an agarose gel containing formaldehyde is transferred to a nylon filter according to standard procedures routinely used in the field (Sambrook and Russell, (2001) above). The expression of RNA encoded by the pesticide gene is then analyzed by hybridizing the filter to a radioactive probe derived from a pesticide gene, using methods known in the field (Sambrook and Russell, (2001) above). Western blot analysis, biochemical assays and similar methods can be performed on transgenic plants to confirm the presence of protein encoded by the pesticide gene using conventional procedures (Sambrook and Russell, 2001, above) by using antibodies that bind to one or more epitopes present in the PIP-72 polypeptide. Stacking of PIP-72 traits and silencing elements in a transgenic plant Transgenic plants may comprise a stack of one or more insecticidal polynucleotides described herein with one or more additional polynucleotides resulting in the production or suppression of multiple insecticidal polypeptide sequences. Transgenic plants comprising polynucleotide sequence clusters may be obtained by traditional plant breeding methods, genetic engineering methods, or both. These methods include, but are not limited to, cultivating individual lines, each comprising a polynucleotide of interest, and transforming a transgenic plant comprising A gene or silencing element described herein may be combined with a subsequent gene or silencing element and cotransformed into a single plant cell. As used herein, the term “stacked” includes having multiple traits present in the same plant (i.e., both traits are incorporated into the nuclear genome, one trait is incorporated into the nuclear genome and one trait is incorporated into the genome of a plastid, or both traits are incorporated into the genome of a plastid). In a non-limiting example, “stacked traits” comprise a molecular stack in which the sequences are physically adjacent to each other. A trait, as used herein, refers to the phenotype derived from a particular sequence or group of sequences.Gene cotransformation can be performed using single transformation vectors comprising multiple genes or multiple vectors carrying the genes separately. If the sequences are grouped by genetic transformation of plants, the polynucleotide sequences of interest can be combined at any time and in any order. Traits can be introduced simultaneously in a simultaneous transformation protocol with the polynucleotides of interest provided by any combination of transformation cassettes. For example, if two sequences are to be introduced, the two sequences can be contained in separate transformation (trans) cassettes or in the same transformation cassette. (cis). The expression of the sequences may be controlled by the same promoter or by different promoters. In certain cases, it may be desirable to introduce a transformation cassette that will suppress the expression of the polynucleotide of interest. This can be combined with any combination of other suppression cassettes or overexpression cassettes to generate the desired combination of characteristics in the plant. It is further recognized that polynucleotide sequences can be clustered at a desired genomic location by means of a site-specific recombination system. See, for example, patents WO 1999 / 25821, WO 1999 / 25854, WO 1999 / 25840, WO 1999 / 25855, and WO 1999 / 25853, all of which are incorporated herein by reference. In some embodiments, one or more polynucleotides encoding the polypeptides of the PIP-72 polypeptide or fragments or variants thereof may be stacked with one or more polynucleotides encoding one or more polypeptides having insecticidal activity or agronomic traits as discussed above and may additionally and optionally include one or more polynucleotides facilitating the silencing of genes of one or more target polynucleotides as described below. In some embodiments, the polynucleotides encoding one or more of the PIP-72 polypeptides described herein are stacked with one or more polynucleotides encoding pesticide proteins described herein. In one embodiment, the polynucleotides encoding one or more of the PIP-72 polypeptides described herein are stacked with one or more polynucleotides encoding the PIP-47 polypeptides of WO2015 / 023846, which are incorporated as a reference in their entirety. Gene silencing In some embodiments, the clustered trait may take the form of silencing one or more polynucleotides of interest, resulting in the suppression of one or more polypeptides in the target pests. In some embodiments, silencing is achieved through the use of a silencing element. In some forms, the polynucleotides encoding the PIP-72 polypeptides described herein are stacked with one or more silencing elements that have insecticidal activity. In some embodiments, the polynucleotides encoding the PIP-72 polypeptides described herein are stacked with one or more polynucleotides encoding the silencing elements targeting RyanR (seq. id. no. 992), HP2 (seq. id. no. 994), or RPS10 (seq. id. no. 995). In one embodiment, the polynucleotides encoding the PIP-72 polypeptides described herein are stacked with polynucleotides encoding a silencing element described in U.S. Patent Application No. US2014 / 0275208 or US2015 / 0257389. In one embodiment, the polynucleotides that The PIP-72 polypeptides described herein are stacked with polynucleotides encoding a silencing element comprising any of sec. ident. no.: 982-991, 993, or sec. ident. no.: 561-572 of the publication of U.S. patent applications no. US2014 / 0275208 and US2015 / 0257389. In some embodiments, the polynucleotides encoding the PIP-72 polypeptides and the polynucleotides encoding the silencing elements described herein are stacked with one or more additional insect-resistant traits. In some embodiments, the polynucleotides encoding the PIP-72 polypeptides and the polynucleotides encoding the silencing elements described herein, which are intended to be stacked with one or more additional insect resistance traits, can be stacked with one or more additional input traits (e.g., herbicide resistance, fungal resistance, virus resistance, stress tolerance, disease resistance, male sterility, stem strength, and the like) or output traits (e.g., increased yield, modified starches, improved oil profile, balanced amino acids, high lysine or methionine content, increased digestibility, improved fiber quality, drought resistance, and the like). Therefore, the polynucleotide embodiments can be used to provide a complete agricultural package of improved crop quality with the ability to flexibly and cost-effectively control any number of agricultural pests. Some methods refer to the negative regulation of the expression of target genes in insect pest species by interfering with ribonucleic acid (RNA) molecules. Silencing elements that can be stacked with one or more PIP-72 polynucleotides include the following: vacuolar H ATPase subunit silencing elements (U.S. patent application publication 2012 / 0198586); insect ribosomal protea such as ribosomal protea L19 (PCT publication no.2012 / 0198586), the L40 ribosomal protein or the S27A ribosomal protein; an insect proteasome subunit such as the Rpn6 protein, the Pros 25 protein, the Rpn2 protein, the beta 1 proteasome subunit protein, or the Pros beta 2 protein; an insect p-coatomer of the COPI vesicle, the Y-coatomer of the COPI vesicle, the P'-coatomer protein, or the Z-coatomer of the COPI vesicle; an insect tetraspanin 2 A protein that is a putative transmembrane domain protein; an insect protein belonging to the actin family, such as Actin 5C; an insect ubiquitin-5E protein; an insect Sec23 protein that is a GTPase activator involved in intracellular protein transport; an insect wrinkle proteme that is an unconventional myosin involved in motor activity; an insect wrinkle-neck proteme that is involved in regulating the cutting and splicing process. alternative nuclear mRNA; an insect vacuolar H+ ATPase G subunit protein and an insect Tbp-1 such as a Tat-binding protein. PCT publication WO 2007 / 035650 describes silencing elements targeting Snf7; US patent application publication 2011 / 0054007 describes polynucleotide silencing elements targeting RPS10. US patent application publication 2015 / 0257389 describes polynucleotide silencing elements targeting RyanR and PAT3; US patent application publication2012 / 0164205 describes silencing elements: a Chd3 homologous sequence, a beta-tubulin homologous sequence, a 40 kDa V-ATPase homologous sequence, an EF1a homologous sequence, a 26S proteasome p28 homologous sequence, a juvenile hormone epoxide hydrolase homologous sequence, a dilatation-dependent chloride channel homologous sequence, a glucose-6-phosphate 1-dehydrogenase homologous sequence, an Act42A homologous sequence, an ADP ribosylation factor 1 homologous sequence, a transcription factor IIB homologous sequence, a chitinase homologous sequence, a ubiquitin-conjugating enzyme homologous sequence, a glyceraldehyde-3-phosphate dehydrogenase homologous sequence, and a ubiquitin B homologous sequence. a homolog of juvenile hormone esterase and a homologous sequence of alpha-tubulin. Pesticide and insecticidal activity “Pest” includes, but is not limited to, insects, fungi, bacteria, nematodes, mites, ticks, and the like. Insect pests include selected insects from the orders Coleoptera, Diptera, Hymenoptera, Lepidoptera, Mallophaga, Homoptera, Hemiptera, Orthoptera, Thysanoptera, Dermaptera, Isoptera, Anoplura, Siphonaptera, Trichoptera, etc., particularly Lepidoptera and Coleoptera. Experts in the field will recognize that not all compounds are equally effective against all pests. The compounds in these formulations show activity against insect pests, which may include economically important agricultural, forestry, greenhouse, ornamental nursery, food and fiber, public and animal health, domestic and commercial, and household and stored product pests. The larvae of the order Lepidoptera include, but are not limited to, armyworms, cutworms, loopers, and heliotines of the family Noctuidae: Spodoptera frugiperda JE Smith (fall armyworm); S. exigua Hubner (beet armyworm); S. litura Fabricius (tobacco gray caterpillar, cotton looper); Mamestra configurata Walker (Bertha armyworm); M. brassicae Linnaeus (cabbage moth); Agrotis ipsilon Hufnagel (cutworm); A. orthogonia Morrison (western cutworm); A. subterranea Fabricius (granular cutworm); Alabama argillacea Hubner (cotton leafworm); Trichoplusia ni Hubner (cabbage looper); Pseudoplusia includens Walker (soybean looper); Anticarsia gemmatalis Hubner (bean caterpillar); Hypena scabra Fabricius (green soybean looper); Heliothis virescens Fabricius (tobacco looper); Pseudaletia unipuncta Haworth (arborworm); Athetis mindara Barnes and Mcdunnough (rough skin cutworm); Euxoa messoria Harris (dark gray cutworm); Earias insulana Boisduval (spiny cotton caterpillar); E. vittella Fabricius (spotted caterpillar); Helicoverpa armigera Hubner (American bollworm); H.Zea Boddie (cotton caterpillar); Melanchra picta Harris (zebra caterpillar); Egira (Xylomyges) curialis Grote (citrus cutworm); borers, bud borers, webworms, pine acorn caterpillars, and skeletonizing caterpillars of the family Pyralidae, Ostrinia nubilalis Hubner (European corn borer); Amyelois transitella Walker (orange navelworm); Anagasta kuehniella Zeller (Mediterranean flour moth); Cadra cautella Walker (almond moth); Chilo suppressalis Walker (rice stem borer); C. partellus (sorghum borer); Corcyra cephalonica Stainton (rice moth); Crambus caliginosellus Clemens (corn root weaver caterpillar); C. teterrellus Zincken (grass weaver worms); Cnaphalocrocis medinalis Guenee (rice leaf roller); Desmia funeralis Hubner (grape roller worm); Diaphania hyalinata Linnaeus (melon worm); D.nitidalis Stoll (cucumber worm); Diatraea grandiosella Dyar (southwest ma^z sweeper), D.saccharalis Fabricius (sugarcane borer); Eoreuma loftini Dyar (Mexican rice borer); Ephestia elutella Hubner (tobacco (cacao) moth); Galleria mellonella Linnaeus (waxworm); Herpetogramma licarsisalis Walker (turf weaver); Homoeosoma electellum Hulst (sunflower moth); Elasmopalpus lignosellus Zeller (lesser cornstalk borer); Achroia grisella Fabricius (lesser wax moth); Loxostege sticticalis Linnaeus (beet moth); Orthaga thyrisalis Walker (tea weaver moth); Maruca testulalis Geyer (pod borer); Plodia interpunctella Hubner (Indian flour moth); Scirpophaga incertulas Walker (yellow stem borer); Udea rubigalis Guenee (celery leafworm); and leaf rollers, bollworms, seedworms and fruitworms of the family Tortricidae, Acleris gloverana Walsingham (western blackheaded bollworm); A.variana Fernald (western black-headed fall armyworm); Archips argyrospila Walker (fruit tree leafroller); A. rosana Linnaeus (European leafroller); and other Archips species, Adoxophyes orana Fischer von Rosslerstamm (fruit skin caterpillar); Cochylis hospes Walsingham (sunflower stripe moth); Cydia latiferreana Walsingham (hazelnut moth); C. pomonella Linnaeus (apple moth); Platynota flavedana Clemens (variegated leafroller); P. stultana Walsingham (ommovorous leafroller); Lobesia botrana Denis & Schiffermuller (European grape berry moth). of the vine); Spilonota ocellana Denis & Schiffermuller (red bud moth); Endopiza viteana Clemens (vine moth); Eupoecilia ambiguella Hubner (grape moth); Bonagota salubricola Meyrick (Brazilian apple leafroller); Grapholita molesta Busck (oriental fruit moth); Suleima helianthana Riley (sunflower bud moth); Argyrotaenia spp.; Choristoneura spp. Other selected agricultural pests of the order Lepidoptera include, but are not limited to, Alsophila pometaria Harris (winter cankerworm); Anarsia lineatella Zeller (peach borer); Anisota senatoria JESmith (orange-striped caterpillar); Antheraea pernyi Guerin-Meneville (Chinese tussah oak moth); Bombyx mori Linnaeus (silkworm); Bucculatrix thurberiella Busck (cotton leaf borer); Colias eurytheme Boisduval (alfalfa caterpillar); Datana integerrima Grote & Robinson (pecan caterpillar); Dendrolimus sibiricus Tschetwerikov (Siberian silk moth); Ennomos subsignaria Hubner (elm caterpillar); Erannis tiliaria Harris (linden looper); Euproctis chrysorrhoea Linnaeus (brown-tailed moth); Harrisina americana Guerin-Meneville (vine leaf stripper); Hemileuca olivee Cockrell (olive looper); Hyphantria cunea Drury (autumn weaver caterpillar); Keiferia lycopersicella Walsingham (tomato pinworm); Lambdina fiscellaria fiscellaria Hulst (eastern hemlock looper); L. fiscellaria lugubrosa Hulst (western hemlock looper); Leucoma salicis Linnaeus (white poplar moth); Lymantria dispar Linnaeus.(Gypsy moth); Manduca quinquemaculata Haworth (five-spotted moth, tomato hornworm); M. sexta Haworth (tomato worm, tobacco worm); Operophtera brumata Linnaeus (winter moth); Paleacrita vernata Peck (spring canker worm); Papilio cresphontes Cramer (giant swallowtail, orange dog); Phryganidia californica Packard (California oakworm); Phyllocnistis citrella Stainton (citrus borer); Phyllonorycter blancardella Fabricius (spotted leaf borer); Pieris brassicae Linnaeus (large white cabbage butterfly); P. rapae Linnaeus (small white cabbage butterfly); P.napi Linnaeus (white-green moth); Platyptilia carduidactyla Riley (artichoke moth); Plutella xylostella Linnaeus (diamond-backed moth); Pectinophora gossypiella Saunders (pink caterpillar); Pontia protodice Boisduval and Leconte (southern cabbage worm); Sabulodes aegrotata Guenee (ommovorous false looper); Schizura concinna JE Smith (red hump caterpillar); Sitotroga cerealella Olivier (Angoumois grain moth); Thaumetopoea pityocampa Schiffermuller (pine processionary caterpillar); Tineola bisselliella Hummel (clothes moth); Tuta absoluta Meyrick (tomato borer). Yponomeuta padella Linnaeus (ermine moth); Heliothis subflexa Guenee; Malacosoma spp. and Orgyia spp. Of interest are the larvae and adults of the order Coleoptera, which includes weevils of the families Anthribidae, Bruchidae, and Curculionidae (which include, but are not limited to: Anthonomus grandis Boheman (cotton weevil); Lissorhoptrus oryzophilus Kuschel (rice water weevil); Sitophilus granarius Linnaeus (wheat weevil); S. oryzae Linnaeus (rice weevil); Hypera punctata Fabricius (clover leaf weevil); Cylindrocopturus adspersus LeConte (sunflower stem weevil); Smicronyx fulvus LeConte (red sunflower seed weevil); S. sordidus LeConte (red sunflower seed weevil); Sphenophorus maidis Chittenden (corn aphid); American flea beetles, cucumber beetle, rootworm, leaf beetles, potato beetles, and leaf borers of the family Chrysomelidae, which include, but are not limited to: Leptinotarsa ​​decemlineata Say (Colorado potato beetle); Diabrotica virgifera virgifera LeConte (western corn rootworm); D. barberi Smith and Lawrence (northern corn rootworm); d.undecimpunctata howardi Barber (southern corn rootworm); Chaetocnema pulicaria Melsheimer (corn beetle); Phyllotreta cruciferae Goeze (cruciferous beetle); Phyllotreta striolata (striped flea beetle); Colaspis brunnea Fabricius (grape colaspis); Oulema melanopus Linnaeus (cereal leaf beetle); Zygogramma exclamationis Fabricius (sunflower beetle)); beetles of the family Coccinellidae (which include, but are not limited to: Epilachna varivestis Mulsant (Mexican bean beetle)); scarabs and other beetles of the family Scarabaeidae (which include, but are not limited to: Popillia japonica Newman (Japanese beetle); Cyclocephala borealis Arrow (northern white grub, white grub); C. immaculata Olivier (southern white grub, white grub);. Rhizotrogus majalis Razoumowsky (European scarab beetle); Phyllophaga crinita Burmeister (white grub); Ligyrus gibbosus De Geer (carrot beetle); carpet beetles of the family Dermestidae; wireworms of the family Elateridae, Eleodes spp., Melanotus spp.; Conoderus spp.; Limonius spp.; Agriotes spp.; Ctenicera spp.; Aeolus spp.; bark beetles or scolytids of the family Scolytidae and beetles of the family Tenebrionidae. Adults and immatures of the order Diptera are of interest, and include leaf borers Agromyza parvicornis Loew (spotted maize leaf borer); midges (which include, but are not limited to: Contarinia sorghicola Coquillett (sorghum midge); Mayetiola destructor Say (Hessian midge); Sitodiplosis mosellana Gehin (wheat midge); Neolasioptera murtfeldtiana Felt, (sunflower seed midge)); fruit flies (Tephritidae), Oscinella frit Linnaeus (fruit flies); larvae (including, but not limited to: Delia platura Meigen (corn seedworm); D. coarctata Fallen (wheat bulbworm) and other Delia spp. species, Meromyza americana Fitch (wheat stemworm); Musca domestica Linnaeus (houseflies); Fannia canicularis Linnaeus, F. femoralis Stein (lesser houseflies); Stomoxys calcitrans Linnaeus (stable fly)); face flies, horn flies, death flies, Chrysomya spp.; Phormia spp.and other pests of muscoid flies, horse flies Tabanus spp.; colmoyotes Gastrophilus spp.; Oestrus spp.; cattle worms. Hypoderma spp.; deer fly Chrysops spp.; Melophagus ovinus Linnaeus (sheep fly) and other Brachycera, mosquitoes Aedes spp.; Anopheles spp.; Culex spp.; black fly Prosimulium spp.; Simulium spp.; midges, sniffing midges, ciarids, and other nematocera. Insects of interest include adults and nymphs of the orders Hemiptera and Homoptera such as, but not limited to, adelgids of the family Adelgidae, plant bugs of the family Miridae, cicadas of the family Cicadidae, jumping insects, Empoasca spp.; of the Cicadellidae family, leafhoppers of the Cixiidae, Flatidae, Fulgoroidea, Issidae and Delphacidae families, treehoppers of the Membracidae family, psyllids of the Psyllidae family, whiteflies of the Aleyrodidae family, aphids of the Aphididae family, phylloxera of the Phylloxeridae family, mealybugs of the Pseudococcidae family, scale insects of the Asterolecanidae, Coccidae, Dactylopiidae, Diaspididae, Eriococcidae, Ortheziidae, Phoenicococcidae and Margarodidae families, lace bugs of the Tingidae family, stink bugs of the Pentatomidae family, bed bugs, Blissus spp.; and other seed bugs of the family Lygaeidae, spittlebugs of the family Cercopidae, squash bugs of the family Coreidae, and red bugs and cotton stainers of the family Pyrrhocoridae. The agronomically important members of the order Homoptera also include, but are not limited to: Acyrthisiphon pisum Harris (pea aphid); Aphis craccivora Koch (legume aphid); A. fabae Scopoli (black bean aphid); A. gossypii Glover (cotton aphid, melon aphid); A. maidiradicis Forbes (corn root aphid); A. pomi De Geer (apple aphid); A. spiraecola Patch (green citrus aphid); Aulacorthum solani Kaltenbach (potato aphid); Chaetosiphon fraga efolii Cockerell (strawberry aphid); Diuraphis noxia Kurdjumov / Mordvilko (Russian wheat aphid); Dysaphis plantaginea Paaserini (apple aphid); Eriosoma lanigerum Hausmann (apple aphid); Brevicoryne brassicae Linnaeus (cabbage aphid); Hyalopterus pruni Geoffroy (plum mealybug); Lipaphis erysimi Kaltenbach (green cabbage aphid); Metopolophium dirrhodum Walker (cereal aphid); Macrosiphum euphorbiae Thomas (potato aphid); Myzus persicae Sulzer (peach-potato aphid, green peach aphid); Nasonovia ribisnigri Mosley (lettuce aphid); Pemphigus spp.(rhizophagous snails and aphid-forming aphids); Rhopalosiphum maidis Fitch (pulgon de la hoja del ma^z); R. padi Linnaeus (thallus pulgon); Schizaphis graminum Rondani (green pulgon of cereals); Sipha flava Forbes (pulgon amarillo de la cana de azucar); Sitobion avenae Fabricius (dark green pulgon de la espiga); Buckton Spotted Therioaphis (missed alfalfa tick); Toxoptera aurantii Boyer de Fonscolombe (pulgon negro de los c^tricos) and T. citricida Kirkaldy (pulgon cafe de los c^tricos); Melanaphis sacchari (flower of the cana de azucar); Adelges spp. (adelgidos); Phylloxera devastatrix Pergande (American nogal phylloxera); Bemisia. tabaci Gennadius (tobacco whitefly, sweet potato whitefly); B. argentifolii Bellows & Perring (silverleaf whitefly); Dialeurodes citri Ashmead (citrus whitefly); Trialeurodes abutiloneus (banded-winged whitefly) and T. vaporariorum Westwood (greenhouse whitefly); Empoasca fabae Harris (potato leafhopper); Laodelphax striatellus Fallen (brown planthopper); Macrolestes quadrilineatus Forbes (aster planthopper); Nephotettix cinticeps Uhler (green planthopper); N. nigropictus Stal (rice planthopper); Nilaparvata lugens Stal (brown planthopper); Peregrinus maidis Ashmead (maize planthopper); Sogatella furcifera Horvath (white-backed manakin); Sogatodes orizicola Muir (rice delfacidae); Typhlocyba pomaria McAtee (white apple leafhopper); Erythroneaura spp.(grape leafhopper); Magicica da septendecim Linnaeus (periodic leafhopper); Icerya purchasi Maskell (cottony scale); Quadraspidiotus perniciosus Comstock (San Jose scale); Planococcus citri Risso (citrus mealy scale); Pseudococcus spp. (another mealybug complex); Cacopsylla pyricola Foerster (pear flea beetle); Trioza diospyri Ashmead (persimmon psyllids). The agronomically important species of the order Hemiptera include, but are not limited to: Acrosternum hilare Say (green stink bug); Anasa tristis De Geer (squash bug); Blissus leucopterus leucopterus Say (stink bug); Corythuca gossypii Fabricius (gossypite bug). encaje del algodonero); Cyrtopeltis modesta Distant (tomate chinche); Dysdercus suturellus Herrich-Schaffer (manchador de la fiber del algodon); Euschistus servus Say (chinche apestosa cafe); E. variolarius Palisot de Beauvois (chinche apestosa manchada); Graptostethus spp. (complejo de chinches de semillas); Leptoglossus corculus Say (pine seedling insect); Lygus lineolaris Palisot de Beauvois (chinche manchadora); L. Hesperus Knight (chinche manchador occidental); L. pratensis Linnaeus (chinche comun del prado); L. rugulipennis Poppius (European chinche manchador); Lygocoris pabulinus Linnaeus (common green capsid); Nezara viridula Linnaeus (surrounding green chinche); Oebalus pugnax Fabricius (arroz chinche apestosa); Oncopeltus fasciatus Dallas (Algodon de seda big chinche); Pseudatomoscelis serietus Reuter (algodonero thorn pulp). In addition, las modalities pueden ser efficacious against los hem^pteros such as, Calocoris norvegicus Gmelin (chinche de la fresa); Orthops plains Linnaeus; Plesiocoris rugicollis Fallen ((capside del manzano); Cyrtopeltis modestus Distant (chinche del tomate); Cyrtopeltis notatatus Distant (mosca chupadora); Spanagonicus albofasciatus Reuter (saltona negra flea); Diaphnocoris chlorionis Say (chinche de la acacia de tres espinas); Labopidicola allii Knight (chinche de la cebolla); Pseudatomoscelis seriatus Reuter (saltona del algodonero flea); Adelphocoris Rapidus Say (False chinche); Nysius raphanus Howard (False chinche); Nezara viridula Linnaeus (green bedbug); Eurygaster spp.; Coreidae spp.; Pyrrhocoridae spp.; Tinidae spp.; Blostomatidae spp.; Reduviidae spp. and Cimicidae spp. In addition, adults and larvae of the order Acari (mites) are included, such as Aceria tosichella Keifer (wheat curl mite); Petrobia latens Muller (brown wheat mite); spider mites and red mites of the family Tetranychidae, Panonychus ulmi Koch (European red mite); Tetranychus urticae Koch (spotted spider mite); (T. mcdanieli McGregor (McDaniel mite); T. cinnabarinus Boisduval (carmine spider mite); T. turkestani Ugarov & Nikolski (strawberry spider mite); flat mites in the family Tenuipalpidae, Brevipalpus lewisi McGregor (citrus flat mite); bud and erinosis mites in the family Eriophyidae and other foliaphagous mites and mites important to the health of humans and animals, for example, dust mites in the family Epidermoptidae, follicle mites in the family Demodicidae, grain mites in the family Glycyphagidae, ticks in the order Ixodidae. Ixodes scapularis Say (black-legged tick); I.holocyclus Neumann (Australian tick that causes paralysis); Dermacentor variabilis Say (American dog tick); Amblyomma americanum Linnaeus (lone star tick) and mange and itch mites of the families Psoroptidae, Pyemotidae and Sarcoptidae. Insect pests of the order Thysanura are of interest, such as Lepisma saccharina Linnaeus (silverfish); Thermobia domestica Packard (fire insect). Other covered arthropod pests include: spiders in the order Araneae such as Loxosceles reclusa Gertsch and Mulaik (brown recluse spider) and Latrodectus mactans Fabricius (black widow spider) and centipedes in the order Scutigeromorpha such as Scutigera coleoptrata Linnaeus (house centipede). Insect pests of interest include the superfamily of stink bugs and other related insects that include, but are not limited to, species belonging to the family Pentatomidae (Nezara viridula, Halyomorpha halys, Piezodorus guildini, Euschistus servus, Acrosternum hilare, Euschistus heros, Euschistus tristigmus, Acrosternum hilare, Dichelops furcatus, Dichelops melacanthus, and Bagrada hilaris (bagrada bug)), the family Plataspidae (Megacopta cribraria - bean bug) and the family Cydnidae (Scaptocoris castanea - root stink bug) and species of Lepidoptera that include, but are not limited to: cabbage moth, e.g., Helicoverpa zea Boddie; soybean looper, e.g. e.g., Pseudoplusia includens Walker and bean velvet caterpillar p. e.g., Anticarsia gemmatalis Hubner. Methods for measuring pesticide activity are well known in this field. See, for example, Czapla and Lang, (1990) J. Econ. Entomol. 83:2480 2485; Andrews, et al., (1988) Biochem. J. 252:199-206; Marrone, et al., (1985) J. of Economic Entomology 78:290-293 and U.S. Patent No. 5,743,477, which are incorporated herein by reference in their entirety. Generally, the protein is mixed and used in feeding trials. See, for example, Marrone, et al., (1985) J. of Economic Entomology 78:290-293. Such trials may include exposing plants to one or more pests and determining the plant's ability to survive and / or kill the pests. Nematodes include parasitic nematodes such as root-knot, cyst, and lesion nematodes, including Heterodera spp., Meloidogyne spp., and Globodera spp.; particularly, the cyst nematode members, which include, but are not limited to, Heterodera glycines (soybean cyst nematode); Heterodera schachtii (beet cyst nematode); Heterodera avenae (cereal cyst nematode); and Globodera rostochiensis and Globodera pailida (potato cyst nematodes). Lesion-causing nematodes include Pratylenchus spp. Seed treatment To protect and enhance production technologies and traits, seed treatment options can provide greater cropping flexibility and cost-effective control of insects, weeds, and diseases. Seed material can typically be surface-treated with a composition comprising combinations of chemical herbicides or Biologicals, protectants, herbicides, insecticides, fungicides, germination inhibitors and enhancers, nutrients, plant growth regulators and activators, bactericides, nematicides, avicides, and / or molluscicides. These compounds are typically formulated with other carriers, surfactants, or adjuvants that enhance application, commonly used in the formulation material. Coatings can be applied by impregnating the propagation material with a liquid formulation or by coating it with a combined wet or dry formulation. Examples of the various types of compounds that can be used as seed treatments are provided in *The Pesticide Manual: A World Compendium*, CDS Tomlin Ed., published by the British Crop Production Council, which is incorporated herein by reference. Some seed treatments that can be used on crop seeds include, but are not limited to, abscisic acid, acibenzolar-S-methyl, avermectin, amitrol, azaconazole, azospiril, azadirachtin, azoxystrobin, Bacillus spp. (which includes one or more species of: cereus, firmus, megaterium, pumilis, sphaericus, subtilis and / or thuringiensis), Bradyrhizobium spp. (which includes one or more of betae, canariense, elkanii, iriomotense, japonicum, liaonigense, pachyrhizi and / or yuanmingense), captan, carboxin, chitosan, clothianidin, copper, ciazipir, difenoconazole, etidiazole, fipronil, fludioxonil, fluoxaestrobin, fluquinconazole, flurazole, fluxofenim, harpine protein, imazalil, imidacloprid, ipconazole, isoflavenoids, lipo-chitooligosaccharide, mancozeb, manganese, maneb, mefenoxam, metalaxyl, metconazole, myclobutanil, PCNB, penflufen, penicillium, penthiopyrad, permethrin, picoxystrobin, prothioconazole, pyraclostrobin, rinaxipyr, S-metolachlor, saponin, sedaxane, TCMTB, tebuconazole, thiabendazole, thiamethoxam, thiocarb, thiram, tolclofos-methyl, triadimenol, trichoderma, trifloxystrobin, triticonazole, and / or zinc. The PCNB seed coating refers to EPA patent number 00293500419, which contains quintozene and terrazole. TCMTB refers to 2-(thiocyanomethylthio)benzothiazole. Seed varieties and seeds with specific transgenic traits can be tested to determine which seed treatment options and application ratios can complement those varieties and transgenic traits to improve production. For example, a variety with good yield potential but susceptibility to ear smut may benefit from a seed treatment that provides protection against ear smut; a variety with good yield potential but susceptibility to the cereal cyst nematode may benefit from a seed treatment that provides protection against the cereal cyst nematode, and so on.Similarly, a variety that includes a transgenic trait that confers insect resistance can benefit from the second mode of action conferred by seed treatment; a variety that includes a transgenic trait that confers herbicide resistance can benefit from seed treatment with a plant protectant that enhances herbicide resistance. plants to that herbicide, etc. In addition, the good root establishment and early emergence that result from the correct use of a seed treatment can result in more efficient nitrogen use, a better ability to withstand drought, and an overall increase in the yield potential of a variety or varieties that contain a certain trait when combined with a seed treatment. Methods for eliminating an insect infestation and controlling an insect population In some embodiments, methods are provided for exterminating an insect pest, comprising contacting the insect pest with an insecticidal amount of a PIP-72 polypeptide and a polynucleotide encoding a silencing element. In some embodiments, methods are provided for exterminating an insect pest, comprising contacting the insect pest with an insecticidal amount of one or more recombinant pesticide proteins from sequence with ID number: 2, sequence with ID number: 4, sequence with ID number: 6, sequence with ID number: 8, sequence with ID number: 10, sequence with ID number: 12, sequence with ID number: 14, sequence with ID number: 18, sequence with ID number: 10, sequence with ID number: 12, sequence with ID number: 14, sequence with ID number: 18, sequence with ID number: 16, sequence with ID number: 17, sequence with ID number: 18, sequence with ID number: 19, sequence with ID number: 10, sequence with ID number: 1 ...1, sequence with ID number: 12, sequence with ID number: 14, sequence with ID number: 18, sequence with ID number: 19, sequence with ID number: 11, sequence with ID number: 12, sequence with ID number: 14, sequence with ID number: 18, sequence with ID number: 16, sequence with ID number: 17, sequence with ID number: 18, sequence with ID number: 19, sequence with ID number of ident.: 28, sec. with ident. no.: 32, any sec. with ident. no.: 528 - sec. with ident. no.: 768, any sec. with ident. no.: 825 - sec. with ident. no.: 844, sec. with ident. no.: 771, sec. with ident. no.: 772 or the sec.with ID number: 852 or one. variant of these, and one or more objective silencing elements described in the publication of U.S. patent application no. US2014 / 0275208 or US2015 / 0257389. In some embodiments, methods are provided for controlling an insect pest population, comprising contacting the insect pest population with an insecticidal amount of one or more recombinant PIP-72 polypeptides and one or more polynucleotides encoding a silencing element. As used herein, “controlling a pest population” or “controlling a pest” refers to any effect on a pest that results in limiting the damage caused by the pest. Controlling a pest includes, but is not limited to, eliminating the pest, inhibiting pest development, altering pest fertility or growth so that the pest causes less damage to the plant, decreasing the number of offspring produced, producing fewer fit pests, producing pests more susceptible to predator attack, or preventing pests from feeding on the plant. In some embodiments, methods are provided for controlling the population of an insect pest resistant to a pesticide protein; the methods comprise contacting the insect pest population with an insecticidal amount of one or more recombinant PIP-72 polypeptides and a silencing element. In some embodiments, methods are provided to protect a plant from an insect pest; the methods comprise expressing in the plant or plant cell a recombinant polynucleotide encoding one or more PIP-72 polypeptides and one or more silencing elements. Strategies for insect resistance management (IRM) Expression of Bacillus thuringiensis 6-endotoxins in transgenic maize plants has been shown to be an effective means of controlling agriculturally important insect pests (Perlak et al., 1990; 1993). However, insects have evolved resistance to the B. thuringiensis 6-endotoxins expressed in transgenic plants. Such resistance, if it becomes widespread, clearly limits the commercial value of germplasm containing the genes encoding these B. thuringiensis 6-endotoxins. One way to increase the effectiveness of transgenic insecticides against target pests and simultaneously reduce the development of insecticide-resistant pests is to provide non-transgenic (i.e., non-insecticidal) refuges (a section of crops / corn without insecticidal effect) for use with transgenic crops that produce an individual insecticidal protein active against the target pests. The U.S. Environmental Protection Agency (epa.gov / oppbppdl / biopesticides / pips / bt_corn_refuge_2006.htm, which can be accessed using the prefix www) publishes the requirements for use with transgenic crops that produce a single Bt protein active against target pests. In addition, the National Corn Growers Association, on its website (ncga.com / insect-resistance-management-fact-sheet-bt-corn, accessible via the www prefix), provides similar guidance regarding refuge requirements. Due to insect losses within the refuge area, larger refuges may reduce overall yield. Another way to increase the effectiveness of transgenic insecticides against target pests and simultaneously reduce the development of insecticide-resistant pests is to have a repository of insecticidal genes that are effective against groups of insect pests and that manifest their effects through different mechanisms of action. Expressing two or more insecticidal compounds toxic to the same insect species in a single plant, with each insecticide expressed at effective levels, is another way to control the development of resistance. This is based on the principle that the evolution of resistance against two independent modes of action is much less likely than against a single one. Roush, for example, describes strategies using two toxins, also called "pyramid" or "cluster" strategies, for managing insecticidal transgenic crops. (The Royal Society. Phil. trans. R. Soc. Lond. B. (1998) 353:1777-1786). The clustering or pyramiding of two different proteins, each effective against the target pests and with little or no resistance to the target pests. No cross-resistance allows for the use of a smaller refuge. The U.S. Environmental Protection Agency requires a significantly less structured refuge (generally 5%) of non-Bt maize to be planted than for single-trait products (generally 20%). There are various ways to provide the IRM effects of a refuge, including various geometric planting patterns in fields and seed mixtures in bags, as further described by Roush. In some configurations, the PIP-72 polypeptides and a polynucleotide encoding a silencing element are useful as an insect resistance management strategy in conjunction (e.g., grouped) with other pesticidal proteins, including, but not limited to, Bt toxins, Xenorhabdus sp. or Photorhabdus sp. insecticidal proteins, and the like. Methods are provided for controlling Lepidoptera and / or Coleoptera insect infestations in a transgenic plant that promotes insect resistance management; the methods comprise expressing in the plant at least two different insecticidal proteins that have different modes of action. In some embodiments, the methods for controlling an infestation of Lepidoptera and / or Coleoptera insects in a transgenic plant and promoting insect resistance management comprise an insecticidal polypeptide PIP-72 and a silencing element for insects of the order Lepidoptera and / or Coleoptera. In some modalities, the methods for controlling the infestation of lepidopteran and / or coleopteran insects in a transgenic plant and promoting insect resistance management include expressing in the transgenic plant a PIP-72 polypeptide and a polynucleotide that encodes the insecticidal silencing element for insects of the order Lepidoptera and / or Coleoptera that have different modes of action. Methods are also provided for reducing the likelihood of the emergence of resistance in lepidopteran and / or coleopteran insects for transgenic plants that express insecticidal proteins to control insect species; the methods comprise the expression of a PIP-72 polypeptide and a polynucleotide encoding an insecticidal silencing element for insect species in conjunction with a second insecticidal protein for insect species that have different modes of action. Furthermore, methods are provided for the effective management of Lepidoptera and / or Coleoptera insect resistance in transgenic plants. These methods comprise co-expressing two or more insecticidal proteins toxic to Lepidoptera and / or Coleoptera at high concentrations in the plants, each exhibiting a distinct mode of extermination. The two or more insecticidal proteins comprise a PIP-72 polypeptide and a Cry protein. Additionally, means are provided for the effective management of Lepidoptera and / or Coleoptera insect resistance in transgenic plants, comprising co-expressing these proteins at high concentrations. in plants two or more insecticidal proteins toxic to Lepidoptera and / or Coleoptera insects but each shows a different way to carry out its extermination activity, where the two or more insecticidal proteins. The foregoing description of the various embodiments illustrated herein is not intended to be exhaustive or to limit the invention to the precise form described. Although specific embodiments and examples are described herein for illustrative purposes, several equivalent modifications are possible within the scope, as will be recognized by those skilled in the relevant art. The lessons provided in the present invention may be applied to purposes other than those described above. The embodiments may be practiced in forms other than those particularly described in the foregoing description and examples. Numerous modifications and variations of the invention are possible in light of the foregoing lessons and are therefore within the scope of the appended claims. These and other changes may be made to the modalities in light of the detailed description above. Generally, in the following claims, the terms used should not be construed as limiting the specific modalities described in the description and the claims. The full description of each cited document (including patents, patent applications, journal articles, abstracts, manuals, books or Other descriptions) in the Introduction, Detailed Description and Examples are incorporated in full into this description by reference. Efforts have been made to ensure accuracy with respect to the numbers used (e.g., quantities, temperatures, concentrations, etc.), but some experimental errors and deviations must be allowed. Unless otherwise stated, parts means parts by weight, molecular weight is the average molecular weight, temperature is in degrees Celsius, and pressure is at or near atmospheric pressure. Experiments Example 1 - Insecticidal Activity of transgenic plants that express PIP-72 and the RyanR dsRNA silencing element The rootworm trials were conducted by infesting plants that had recently been transplanted from the ground into pots with a volume of approximately 3 liters. The soil mix was variable but had to be rich in peat, bark chips, and other soil amendments to lighten the medium and promote healthy root growth and aeration. Two days after transplanting, the plants were infested with 200 western corn rootworm eggs suspended in water. The eggs were timed so that hatching would occur within a few days of infestation. The plants were maintained according to standard greenhouse practices for watering and fertilizer applications. Nineteen days later, the plants were removed from the pots, and the soil was stripped of the eggs. roots to expose feeding damage. Ratings were made using the Node Injury Scale developed by Nowatzki et al (2005) J. of Economic Entomology, 98, 1-8. The Node Injury Score is based on the number of damaged root nodes where 0 indicates no damage and 3 indicates that 3 root nodes were eaten to a length of less than 2 centimeters. Stacked constructs show a significant reduction in feeding damage compared to negative controls (Figure 1). Example 2 - Expression of the RyanR dsRNA silencing element in PIP-72 and the RyanR dsRNA silencing element in stacked transgenic maize The QuantiGene® Plex 2.0 RNA assay (Affymetrix®) was used to detect RyanR-oriented dsRNA (DvSSJ, sequence ID: 993) transcript coding strand in transgenic plants. RyanR-oriented double-stranded RNA was prepared by in vitro transcription. The purified dsRNA was quantified by OD260 and used as a standard for quantitative detection. Transgenic roots (approximately 45 mg) were collected from each individual T0 plant and processed for QuantiGene® detection according to the QuantiGene® 2.0 user manual. RNA expression data were calculated as picograms per mg of fresh root (or pg / mg). Stacked constructs show significant RyanR-oriented dsRNA expression, with no detection in a negative control (Figure 2). Example 3 - Expression of the PIP-72 polypeptide in PIP-72 and of the RyanR dsRNA silencing element in stacked transgenic ma^z The absolute expression concentration of PIP-72Aa proteins was determined using LC-MS / MS (liquid chromatography coupled with mass spectrometry) according to J Agric Food Chem. 2011 Apr 27; 59(8):3551-8. After lyophilization and grinding, 10 mg of leaf samples were extracted with 600 µL of TBST buffer (phosphate-buffered saline with 0.05% Tween 20). Approximately 500 mg of fresh frozen root samples were extracted with 1000 µL of PBST buffer. After centrifugation, the supernatant was collected, and the total extracted proteins (TEPs) were measured using a Bradford assay. The samples were normalized by TEP. A total of 50 pL of the normalized extract was combined with 100 pL of ABCT digestion buffer (100 mM ammonium bicarbonate and 0.05% Tween 20). A standard curve was prepared by loading different amounts of the recombinant protein standard into 50 pL aliquots of the negative sample extract.An appropriate amount of ABCT digestion buffer was added to each point on the standard curve to maintain consistent total volumes between samples and standards. Samples and standards were reduced with 6 pL of 0.25 M dithiothreitol at 50 °C for 30 min and then alkylated with 6 pL of 0.3 M iodoacetamide at room temperature in the dark for 30 min. One pg of trypsin (10 pL) was added to each sample, and digestion was allowed to proceed at 37 °C overnight (~18 hours) before adding 10 pL of 10% iodoacetamide. (v / v) of formic acid. The PIP-72Aa protein was quantified by monitoring its signature peptide QETWDR with MRM (multiple reaction monitoring) transition of 417.7 / 577.3, using a Waters UPLC (ultra-performance liquid chromatography) coupled with an AB SCIEX Q-TRAP 5500. The autosampler temperature was maintained at 8 °C during the analysis. 10 pL volumes were injected into a BEH 50 x 2.1 mm 1.7 p C18 column (Waters) maintained at 60 °C. The mobile phases consisted of 0.1% formic acid (MPA) and 0.1% formic acid in acetonitrile (MPB), and LC was performed at a flow rate of 1.0 mL / min with a linear gradient of 2–10% MPB over 1.5 min. Protein concentrations in the unknown samples were calculated by interpolation on the standard curve using Analyst software version 1.6.2 (AB Sciex). The stacked constructs show significant expression of PIP-72, with no detection in a negative control (Figure 3). Example 4. Stable transformation of maize mediated by Agrobacterium For the Agrobacterium-mediated transformation of maize of PIP-72 and the dsRNA silencing element RyanR into stacked transgenic maize, the Zhao method was employed (U.S. patent no. 5,981,840 and international patent publication no. WO 1998 / 32326). In summary, immature embryos were isolated from maize and the embryos were brought into contact with an Agrobacterium suspension, where the bacteria were able to transfer a polynucleotide encoding a PIP-72 polypeptide and a polynucleotide that It encodes a RyanR-targeted silencing element for at least one cell from at least one of the immature embryos (Stage 1: the infection stage). In this stage, the immature embryos were immersed in an Agrobacterium suspension to initiate inoculation. The embryos were co-cultured for a period with the Agrobacterium (Stage 2: the co-culture stage). The immature embryos were cultured in solid medium with an antibiotic, but without a selective agent, to eliminate the Agrobacterium and for a resting phase for the infected cells. Subsequently, the inoculated embryos were cultured in a medium containing a selective agent, and the transformed callus was recovered (Stage 4: the selection stage). The immature embryos are cultured in a solid medium with a selective agent that produces selective growth of the transformed cells.Then the callus was regenerated in plants (stage 5: the regeneration stage), and calluses were grown in selective media on a solid medium, to regenerate the plants. Transgenic maize plants that are positive for the expression of insecticidal proteins are analyzed for pesticidal activity using standard bioassays known in the field. Such methods include, for example, root excision bioassays and whole-plant bioassays. See, for example, the publication of U.S. patent application no. US 2003 / 0120054 and International publication no. WO 2003 / 018810. IP LEGAL SRL - 30714387304 Digitally signed by PORTALTRAMITES - INPI Date: 2021.01.15 16:13:29 -03:00 Reason: Digitally Signed by the INPI Location: Buenos Aires, Argentina 1253591 187 of 187

Claims

1. An isolated DNA construct characterized in that it comprises i) a nucleic acid molecule encoding a polypeptide having the sequence specified in SEQ ID NO: 2, wherein the polypeptide has insecticidal activity against a Diabrotica species, ii) a silencing element oriented to the sequence specified in SEQ ID NO: 993, wherein the silencing element has insecticidal activity against a Diabrotica species, wherein the nucleic acid molecule is operatively linked to a heterologous regulatory element. Three claims follow.