The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein
Identifieur interne : 000388 ( Pmc/Corpus ); précédent : 000387; suivant : 000389The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein
Auteurs : Ann-Maree Catanzariti ; Peter N. Dodds ; Thomas Ve ; Bostjan Kobe ; Jeffrey G. Ellis ; Brian J. StaskawiczSource :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ] ; 2010.
Abstract
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.
Url:
DOI: 10.1094/MPMI-23-1-0049
PubMed: 19958138
PubMed Central: 3142614
Links to Exploration step
PMC:3142614Le document en format XML
<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)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/MelampsoraV2/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000388 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000388 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= MelampsoraV2 |flux= Pmc |étape= Corpus |type= RBID |clé= PMC:3142614 |texte= The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/RBID.i -Sk "pubmed:19958138" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a MelampsoraV2
This area was generated with Dilib version V0.6.38. |