The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.
Identifieur interne : 003468 ( PubMed/Corpus ); précédent : 003467; suivant : 003469The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.
Auteurs : Stella Césari ; Hiroyuki Kanzaki ; Tadashi Fujiwara ; Maud Bernoux ; Véronique Chalvon ; Yoji Kawano ; Ko Shimamoto ; Peter Dodds ; Ryohei Terauchi ; Thomas KrojSource :
- The EMBO journal [ 1460-2075 ] ; 2014.
English descriptors
- KwdEn :
- Cell Death, Disease Resistance, Magnaporthe (growth & development), Magnaporthe (immunology), Models, Biological, Oryza (immunology), Oryza (microbiology), Plant Proteins (immunology), Plant Proteins (metabolism), Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protoplasts (physiology), Tobacco (immunology), Tobacco (microbiology).
- MESH :
- chemical , immunology : Plant Proteins.
- growth & development : Magnaporthe.
- immunology : Magnaporthe, Oryza, Tobacco.
- chemical , metabolism : Plant Proteins.
- microbiology : Oryza, Tobacco.
- physiology : Protoplasts.
- Cell Death, Disease Resistance, Models, Biological, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping.
Abstract
Plant resistance proteins of the class of nucleotide-binding and leucine-rich repeat domain proteins (NB-LRRs) are immune sensors which recognize pathogen-derived molecules termed avirulence (AVR) proteins. We show that RGA4 and RGA5, two NB-LRRs from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA4 triggers an AVR-independent cell death that is repressed in the presence of RGA5 in both rice protoplasts and Nicotiana benthamiana. Upon recognition of the pathogen effector AVR-Pia by direct binding to RGA5, repression is relieved and cell death occurs. RGA4 and RGA5 form homo- and hetero-complexes and interact through their coiled-coil domains. Localization studies in rice protoplast suggest that RGA4 and RGA5 localize to the cytosol. Upon recognition of AVR-Pia, neither RGA4 nor RGA5 is re-localized to the nucleus. These results establish a model for the interaction of hetero-pairs of NB-LRRs in plants: RGA4 mediates cell death activation, while RGA5 acts as a repressor of RGA4 and as an AVR receptor.
DOI: 10.15252/embj.201487923
PubMed: 25024433
Links to Exploration step
pubmed:25024433Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.</title><author><name sortKey="Cesari, Stella" sort="Cesari, Stella" uniqKey="Cesari S" first="Stella" last="Césari">Stella Césari</name><affiliation><nlm:affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France CSIRO Plant Industry, Canberra, ACT, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Kanzaki, Hiroyuki" sort="Kanzaki, Hiroyuki" uniqKey="Kanzaki H" first="Hiroyuki" last="Kanzaki">Hiroyuki Kanzaki</name><affiliation><nlm:affiliation>Iwate Biotechnology Research Center, Kitakami Iwate, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Fujiwara, Tadashi" sort="Fujiwara, Tadashi" uniqKey="Fujiwara T" first="Tadashi" last="Fujiwara">Tadashi Fujiwara</name><affiliation><nlm:affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Bernoux, Maud" sort="Bernoux, Maud" uniqKey="Bernoux M" first="Maud" last="Bernoux">Maud Bernoux</name><affiliation><nlm:affiliation>CSIRO Plant Industry, Canberra, ACT, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Chalvon, Veronique" sort="Chalvon, Veronique" uniqKey="Chalvon V" first="Véronique" last="Chalvon">Véronique Chalvon</name><affiliation><nlm:affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Kawano, Yoji" sort="Kawano, Yoji" uniqKey="Kawano Y" first="Yoji" last="Kawano">Yoji Kawano</name><affiliation><nlm:affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Shimamoto, Ko" sort="Shimamoto, Ko" uniqKey="Shimamoto K" first="Ko" last="Shimamoto">Ko Shimamoto</name><affiliation><nlm:affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Dodds, Peter" sort="Dodds, Peter" uniqKey="Dodds P" first="Peter" last="Dodds">Peter Dodds</name><affiliation><nlm:affiliation>CSIRO Plant Industry, Canberra, ACT, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Terauchi, Ryohei" sort="Terauchi, Ryohei" uniqKey="Terauchi R" first="Ryohei" last="Terauchi">Ryohei Terauchi</name><affiliation><nlm:affiliation>Iwate Biotechnology Research Center, Kitakami Iwate, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kroj, Thomas" sort="Kroj, Thomas" uniqKey="Kroj T" first="Thomas" last="Kroj">Thomas Kroj</name><affiliation><nlm:affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France thomas.kroj@supagro.inra.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25024433</idno><idno type="pmid">25024433</idno><idno type="doi">10.15252/embj.201487923</idno><idno type="wicri:Area/PubMed/Corpus">003468</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003468</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.</title><author><name sortKey="Cesari, Stella" sort="Cesari, Stella" uniqKey="Cesari S" first="Stella" last="Césari">Stella Césari</name><affiliation><nlm:affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France CSIRO Plant Industry, Canberra, ACT, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Kanzaki, Hiroyuki" sort="Kanzaki, Hiroyuki" uniqKey="Kanzaki H" first="Hiroyuki" last="Kanzaki">Hiroyuki Kanzaki</name><affiliation><nlm:affiliation>Iwate Biotechnology Research Center, Kitakami Iwate, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Fujiwara, Tadashi" sort="Fujiwara, Tadashi" uniqKey="Fujiwara T" first="Tadashi" last="Fujiwara">Tadashi Fujiwara</name><affiliation><nlm:affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Bernoux, Maud" sort="Bernoux, Maud" uniqKey="Bernoux M" first="Maud" last="Bernoux">Maud Bernoux</name><affiliation><nlm:affiliation>CSIRO Plant Industry, Canberra, ACT, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Chalvon, Veronique" sort="Chalvon, Veronique" uniqKey="Chalvon V" first="Véronique" last="Chalvon">Véronique Chalvon</name><affiliation><nlm:affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Kawano, Yoji" sort="Kawano, Yoji" uniqKey="Kawano Y" first="Yoji" last="Kawano">Yoji Kawano</name><affiliation><nlm:affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Shimamoto, Ko" sort="Shimamoto, Ko" uniqKey="Shimamoto K" first="Ko" last="Shimamoto">Ko Shimamoto</name><affiliation><nlm:affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Dodds, Peter" sort="Dodds, Peter" uniqKey="Dodds P" first="Peter" last="Dodds">Peter Dodds</name><affiliation><nlm:affiliation>CSIRO Plant Industry, Canberra, ACT, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Terauchi, Ryohei" sort="Terauchi, Ryohei" uniqKey="Terauchi R" first="Ryohei" last="Terauchi">Ryohei Terauchi</name><affiliation><nlm:affiliation>Iwate Biotechnology Research Center, Kitakami Iwate, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kroj, Thomas" sort="Kroj, Thomas" uniqKey="Kroj T" first="Thomas" last="Kroj">Thomas Kroj</name><affiliation><nlm:affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France thomas.kroj@supagro.inra.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The EMBO journal</title><idno type="eISSN">1460-2075</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Death</term><term>Disease Resistance</term><term>Magnaporthe (growth & development)</term><term>Magnaporthe (immunology)</term><term>Models, Biological</term><term>Oryza (immunology)</term><term>Oryza (microbiology)</term><term>Plant Proteins (immunology)</term><term>Plant Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Interaction Mapping</term><term>Protoplasts (physiology)</term><term>Tobacco (immunology)</term><term>Tobacco (microbiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Magnaporthe</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Magnaporthe</term><term>Oryza</term><term>Tobacco</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Oryza</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protoplasts</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Death</term><term>Disease Resistance</term><term>Models, Biological</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Interaction Mapping</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant resistance proteins of the class of nucleotide-binding and leucine-rich repeat domain proteins (NB-LRRs) are immune sensors which recognize pathogen-derived molecules termed avirulence (AVR) proteins. We show that RGA4 and RGA5, two NB-LRRs from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA4 triggers an AVR-independent cell death that is repressed in the presence of RGA5 in both rice protoplasts and Nicotiana benthamiana. Upon recognition of the pathogen effector AVR-Pia by direct binding to RGA5, repression is relieved and cell death occurs. RGA4 and RGA5 form homo- and hetero-complexes and interact through their coiled-coil domains. Localization studies in rice protoplast suggest that RGA4 and RGA5 localize to the cytosol. Upon recognition of AVR-Pia, neither RGA4 nor RGA5 is re-localized to the nucleus. These results establish a model for the interaction of hetero-pairs of NB-LRRs in plants: RGA4 mediates cell death activation, while RGA5 acts as a repressor of RGA4 and as an AVR receptor.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25024433</PMID><DateCreated><Year>2014</Year><Month>09</Month><Day>02</Day></DateCreated><DateCompleted><Year>2014</Year><Month>10</Month><Day>28</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2075</ISSN><JournalIssue CitedMedium="Internet"><Volume>33</Volume><Issue>17</Issue><PubDate><Year>2014</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J.</ISOAbbreviation></Journal><ArticleTitle>The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.</ArticleTitle><Pagination><MedlinePgn>1941-59</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.15252/embj.201487923</ELocationID><Abstract><AbstractText>Plant resistance proteins of the class of nucleotide-binding and leucine-rich repeat domain proteins (NB-LRRs) are immune sensors which recognize pathogen-derived molecules termed avirulence (AVR) proteins. We show that RGA4 and RGA5, two NB-LRRs from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA4 triggers an AVR-independent cell death that is repressed in the presence of RGA5 in both rice protoplasts and Nicotiana benthamiana. Upon recognition of the pathogen effector AVR-Pia by direct binding to RGA5, repression is relieved and cell death occurs. RGA4 and RGA5 form homo- and hetero-complexes and interact through their coiled-coil domains. Localization studies in rice protoplast suggest that RGA4 and RGA5 localize to the cytosol. Upon recognition of AVR-Pia, neither RGA4 nor RGA5 is re-localized to the nucleus. These results establish a model for the interaction of hetero-pairs of NB-LRRs in plants: RGA4 mediates cell death activation, while RGA5 acts as a repressor of RGA4 and as an AVR receptor.</AbstractText><CopyrightInformation>© 2014 The Authors.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Césari</LastName><ForeName>Stella</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France CSIRO Plant Industry, Canberra, ACT, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kanzaki</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Iwate Biotechnology Research Center, Kitakami Iwate, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fujiwara</LastName><ForeName>Tadashi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bernoux</LastName><ForeName>Maud</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>CSIRO Plant Industry, Canberra, ACT, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chalvon</LastName><ForeName>Véronique</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kawano</LastName><ForeName>Yoji</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shimamoto</LastName><ForeName>Ko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Takayama Ikoma, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dodds</LastName><ForeName>Peter</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>CSIRO Plant Industry, Canberra, ACT, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Terauchi</LastName><ForeName>Ryohei</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Iwate Biotechnology Research Center, Kitakami Iwate, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kroj</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>INRA UMR BGPI, Montpellier, France CIRAD UMR BGPI, Montpellier, France thomas.kroj@supagro.inra.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>07</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO J</MedlineTA><NlmUniqueID>8208664</NlmUniqueID><ISSNLinking>0261-4189</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):8024-9</RefSource><PMID Version="1">12788974</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Plant Cell. 2000 Dec;12(12):2541-2554</RefSource><PMID Version="1">11148296</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2404-9</RefSource><PMID 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MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025941" MajorTopicYN="N">Protein Interaction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011523" MajorTopicYN="N">Protoplasts</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4195788</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Magnaporthe oryzae</Keyword><Keyword MajorTopicYN="N">pathogen recognition</Keyword><Keyword MajorTopicYN="N">plant immunity</Keyword><Keyword MajorTopicYN="N">resistance protein</Keyword><Keyword MajorTopicYN="N">rice</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>10</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25024433</ArticleId><ArticleId IdType="pii">embj.201487923</ArticleId><ArticleId IdType="doi">10.15252/embj.201487923</ArticleId><ArticleId IdType="pmc">PMC4195788</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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