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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein</title><author><name sortKey="Catanzariti, Ann Maree" sort="Catanzariti, Ann Maree" uniqKey="Catanzariti A" first="Ann-Maree" last="Catanzariti">Ann-Maree Catanzariti</name><affiliation><nlm:aff id="A1"> Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley 94720-3102, U.S.A</nlm:aff></affiliation></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N." last="Dodds">Peter N. Dodds</name><affiliation><nlm:aff id="A2"> Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia</nlm:aff></affiliation></author><author><name sortKey="Ve, Thomas" sort="Ve, Thomas" uniqKey="Ve T" first="Thomas" last="Ve">Thomas Ve</name><affiliation><nlm:aff id="A3"> School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia</nlm:aff></affiliation></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name><affiliation><nlm:aff id="A3"> School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia</nlm:aff></affiliation></author><author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G." last="Ellis">Jeffrey G. Ellis</name><affiliation><nlm:aff id="A2"> Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia</nlm:aff></affiliation></author><author><name sortKey="Staskawicz, Brian J" sort="Staskawicz, Brian J" uniqKey="Staskawicz B" first="Brian J." last="Staskawicz">Brian J. Staskawicz</name><affiliation><nlm:aff id="A1"> Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley 94720-3102, U.S.A</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19958138</idno><idno type="pmc">3142614</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3142614</idno><idno type="RBID">PMC:3142614</idno><idno type="doi">10.1094/MPMI-23-1-0049</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">000388</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000388</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein</title><author><name sortKey="Catanzariti, Ann Maree" sort="Catanzariti, Ann Maree" uniqKey="Catanzariti A" first="Ann-Maree" last="Catanzariti">Ann-Maree Catanzariti</name><affiliation><nlm:aff id="A1"> Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley 94720-3102, U.S.A</nlm:aff></affiliation></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N." last="Dodds">Peter N. Dodds</name><affiliation><nlm:aff id="A2"> Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia</nlm:aff></affiliation></author><author><name sortKey="Ve, Thomas" sort="Ve, Thomas" uniqKey="Ve T" first="Thomas" last="Ve">Thomas Ve</name><affiliation><nlm:aff id="A3"> School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia</nlm:aff></affiliation></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name><affiliation><nlm:aff id="A3"> School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia</nlm:aff></affiliation></author><author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G." last="Ellis">Jeffrey G. Ellis</name><affiliation><nlm:aff id="A2"> Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia</nlm:aff></affiliation></author><author><name sortKey="Staskawicz, Brian J" sort="Staskawicz, Brian J" uniqKey="Staskawicz B" first="Brian J." last="Staskawicz">Brian J. Staskawicz</name><affiliation><nlm:aff id="A1"> Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley 94720-3102, U.S.A</nlm:aff></affiliation></author></analytic><series><title level="j">Molecular plant-microbe interactions : MPMI</title><idno type="ISSN">0894-0282</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M–AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.</p></div></front></TEI><pmc article-type="research-article" xml:lang="en"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">9107902</journal-id><journal-id journal-id-type="pubmed-jr-id">1276</journal-id><journal-id journal-id-type="nlm-ta">Mol Plant Microbe Interact</journal-id><journal-title-group><journal-title>Molecular plant-microbe interactions : MPMI</journal-title></journal-title-group><issn pub-type="ppub">0894-0282</issn></journal-meta><article-meta><article-id pub-id-type="pmid">19958138</article-id><article-id pub-id-type="pmc">3142614</article-id><article-id pub-id-type="doi">10.1094/MPMI-23-1-0049</article-id><article-id pub-id-type="manuscript">NIHMS307074</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Catanzariti</surname><given-names>Ann-Maree</given-names></name><xref rid="A1" ref-type="aff">1</xref></contrib><contrib contrib-type="author"><name><surname>Dodds</surname><given-names>Peter N.</given-names></name><xref rid="A2" ref-type="aff">2</xref></contrib><contrib contrib-type="author"><name><surname>Ve</surname><given-names>Thomas</given-names></name><xref rid="A3" ref-type="aff">3</xref></contrib><contrib contrib-type="author"><name><surname>Kobe</surname><given-names>Bostjan</given-names></name><xref rid="A3" ref-type="aff">3</xref></contrib><contrib contrib-type="author"><name><surname>Ellis</surname><given-names>Jeffrey G.</given-names></name><xref rid="A2" ref-type="aff">2</xref></contrib><contrib contrib-type="author"><name><surname>Staskawicz</surname><given-names>Brian J.</given-names></name><xref rid="A1" ref-type="aff">1</xref></contrib></contrib-group><aff id="A1"><label>1</label> Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley 94720-3102, U.S.A</aff><aff id="A2"><label>2</label> Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia</aff><aff id="A3"><label>3</label> School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia</aff><author-notes><corresp id="FN1">Corresponding author: B. J. Staskawicz; Telephone: +1 510 642 3721; Fax: +1 510 642 4995; <email>stask@berkeley.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>29</day><month>6</month><year>2011</year></pub-date><pub-date pub-type="ppub"><month>1</month><year>2010</year></pub-date><pub-date pub-type="pmc-release"><day>25</day><month>7</month><year>2011</year></pub-date><volume>23</volume><issue>1</issue><fpage>49</fpage><lpage>57</lpage><permissions><copyright-statement>© 2010 The American Phytopathological Society</copyright-statement><copyright-year>2010</copyright-year></permissions><abstract><p id="P1">In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M–AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.</p></abstract><funding-group><award-group><funding-source country="United States">National Institute of General Medical Sciences : NIGMS</funding-source><award-id>R01 GM074265-01A2 || GM</award-id></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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