Stepwise artificial evolution of a plant disease resistance gene.
Identifieur interne : 002378 ( Main/Curation ); précédent : 002377; suivant : 002379Stepwise artificial evolution of a plant disease resistance gene.
Auteurs : C Jake Harris [Royaume-Uni] ; Erik J. Slootweg ; Aska Goverse ; David C. BaulcombeSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2013.
Descripteurs français
- KwdFr :
- Agriculture (méthodes), Agrobacterium tumefaciens (MeSH), Carlavirus (génétique), Gènes vpr (génétique), Génie génétique (méthodes), Immunité innée (génétique), Protéines (génétique), Protéines (immunologie), Protéines de capside (génétique), Protéines végétales (génétique), Protéines végétales (immunologie), RT-PCR (MeSH), Substitution d'acide aminé (génétique), Tabac (génétique), Tabac (immunologie), Tabac (virologie), Technique de Western (MeSH), Végétaux génétiquement modifiés (MeSH).
- MESH :
- génétique : Carlavirus, Gènes vpr, Immunité innée, Protéines, Protéines de capside, Protéines végétales, Substitution d'acide aminé, Tabac.
- immunologie : Protéines, Protéines végétales, Tabac.
- méthodes : Agriculture, Génie génétique.
- virologie : Tabac.
- Agrobacterium tumefaciens, RT-PCR, Technique de Western, Végétaux génétiquement modifiés.
English descriptors
- KwdEn :
- Agriculture (methods), Agrobacterium tumefaciens (MeSH), Amino Acid Substitution (genetics), Blotting, Western (MeSH), Capsid Proteins (genetics), Carlavirus (genetics), Genes, vpr (genetics), Genetic Engineering (methods), Immunity, Innate (genetics), Plant Proteins (genetics), Plant Proteins (immunology), Plants, Genetically Modified (MeSH), Proteins (genetics), Proteins (immunology), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Tobacco (genetics), Tobacco (immunology), Tobacco (virology).
- MESH :
- chemical , genetics : Capsid Proteins, Plant Proteins, Proteins.
- genetics : Amino Acid Substitution, Carlavirus, Genes, vpr, Immunity, Innate, Tobacco.
- chemical , immunology : Plant Proteins, Proteins, Tobacco.
- methods : Agriculture, Genetic Engineering.
- virology : Tobacco.
- Agrobacterium tumefaciens, Blotting, Western, Plants, Genetically Modified, Reverse Transcriptase Polymerase Chain Reaction.
Abstract
Genes encoding plant nucleotide-binding leucine-rich repeat (NB-LRR) proteins confer dominant resistance to diverse pathogens. The wild-type potato NB-LRR protein Rx confers resistance against a single strain of potato virus X (PVX), whereas LRR mutants protect against both a second PVX strain and the distantly related poplar mosaic virus (PopMV). In one of the Rx mutants there was a cost to the broad-spectrum resistance because the response to PopMV was transformed from a mild disease on plants carrying wild-type Rx to a trailing necrosis that killed the plant. To explore the use of secondary mutagenesis to eliminate this cost of broad-spectrum resistance, we performed random mutagenesis of the N-terminal domains of this broad-recognition version of Rx and isolated four mutants with a stronger response against the PopMV coat protein due to enhanced activation sensitivity. These mutations are located close to the nucleotide-binding pocket, a highly conserved structure that likely controls the "switch" between active and inactive NB-LRR conformations. Stable transgenic plants expressing one of these versions of Rx are resistant to the strains of PVX and the PopMV that previously caused trailing necrosis. We conclude from this work that artificial evolution of NB-LRR disease resistance genes in crops can be enhanced by modification of both activation and recognition phases, to both accentuate the positive and eliminate the negative aspects of disease resistance.
DOI: 10.1073/pnas.1311134110
PubMed: 24324167
PubMed Central: PMC3876221
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The wild-type potato NB-LRR protein Rx confers resistance against a single strain of potato virus X (PVX), whereas LRR mutants protect against both a second PVX strain and the distantly related poplar mosaic virus (PopMV). In one of the Rx mutants there was a cost to the broad-spectrum resistance because the response to PopMV was transformed from a mild disease on plants carrying wild-type Rx to a trailing necrosis that killed the plant. To explore the use of secondary mutagenesis to eliminate this cost of broad-spectrum resistance, we performed random mutagenesis of the N-terminal domains of this broad-recognition version of Rx and isolated four mutants with a stronger response against the PopMV coat protein due to enhanced activation sensitivity. These mutations are located close to the nucleotide-binding pocket, a highly conserved structure that likely controls the "switch" between active and inactive NB-LRR conformations. Stable transgenic plants expressing one of these versions of Rx are resistant to the strains of PVX and the PopMV that previously caused trailing necrosis. We conclude from this work that artificial evolution of NB-LRR disease resistance genes in crops can be enhanced by modification of both activation and recognition phases, to both accentuate the positive and eliminate the negative aspects of disease resistance. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24324167</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>110</Volume><Issue>52</Issue><PubDate><Year>2013</Year><Month>Dec</Month><Day>24</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Stepwise artificial evolution of a plant disease resistance gene.</ArticleTitle><Pagination><MedlinePgn>21189-94</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1311134110</ELocationID><Abstract><AbstractText>Genes encoding plant nucleotide-binding leucine-rich repeat (NB-LRR) proteins confer dominant resistance to diverse pathogens. The wild-type potato NB-LRR protein Rx confers resistance against a single strain of potato virus X (PVX), whereas LRR mutants protect against both a second PVX strain and the distantly related poplar mosaic virus (PopMV). In one of the Rx mutants there was a cost to the broad-spectrum resistance because the response to PopMV was transformed from a mild disease on plants carrying wild-type Rx to a trailing necrosis that killed the plant. To explore the use of secondary mutagenesis to eliminate this cost of broad-spectrum resistance, we performed random mutagenesis of the N-terminal domains of this broad-recognition version of Rx and isolated four mutants with a stronger response against the PopMV coat protein due to enhanced activation sensitivity. These mutations are located close to the nucleotide-binding pocket, a highly conserved structure that likely controls the "switch" between active and inactive NB-LRR conformations. Stable transgenic plants expressing one of these versions of Rx are resistant to the strains of PVX and the PopMV that previously caused trailing necrosis. We conclude from this work that artificial evolution of NB-LRR disease resistance genes in crops can be enhanced by modification of both activation and recognition phases, to both accentuate the positive and eliminate the negative aspects of disease resistance. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Harris</LastName><ForeName>C Jake</ForeName><Initials>CJ</Initials><AffiliationInfo><Affiliation>Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Slootweg</LastName><ForeName>Erik J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Goverse</LastName><ForeName>Aska</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Baulcombe</LastName><ForeName>David C</ForeName><Initials>DC</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>12</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D036022">Capsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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