Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p
Identifieur interne : 000857 ( Pmc/Curation ); précédent : 000856; suivant : 000858Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p
Auteurs : Virginie Redeker [France] ; Chris Hughes [Royaume-Uni] ; Jimmy Savistchenko [France] ; Johannes P. C. Vissers [Royaume-Uni] ; Ronald Melki [France]Source :
- PLoS ONE [ 1932-6203 ] ; 2011.
Abstract
The aggregation of the baker's yeast prion Sup35p is at the origin of the transmissible [
We designed a functional proteomic study that combines two techniques to identify modulators of Sup35p aggregation and describe the changes associated to [
Our functional proteomic study provides the first inventory list of over 300 proteins that directly or indirectly affect Sup35p aggregation and [
Url:
DOI: 10.1371/journal.pone.0023659
PubMed: 21931608
PubMed Central: 3172207
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p</title><author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Hughes, Chris" sort="Hughes, Chris" uniqKey="Hughes C" first="Chris" last="Hughes">Chris Hughes</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Waters Corporation, Atlas Park, Manchester, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Waters Corporation, Atlas Park, Manchester</wicri:regionArea></affiliation></author><author><name sortKey="Savistchenko, Jimmy" sort="Savistchenko, Jimmy" uniqKey="Savistchenko J" first="Jimmy" last="Savistchenko">Jimmy Savistchenko</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Vissers, Johannes P C" sort="Vissers, Johannes P C" uniqKey="Vissers J" first="Johannes P. C." last="Vissers">Johannes P. C. Vissers</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Waters Corporation, Atlas Park, Manchester, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Waters Corporation, Atlas Park, Manchester</wicri:regionArea></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21931608</idno><idno type="pmc">3172207</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3172207</idno><idno type="RBID">PMC:3172207</idno><idno type="doi">10.1371/journal.pone.0023659</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000860</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000860</idno><idno type="wicri:Area/Pmc/Curation">000857</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000857</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p</title><author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Hughes, Chris" sort="Hughes, Chris" uniqKey="Hughes C" first="Chris" last="Hughes">Chris Hughes</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Waters Corporation, Atlas Park, Manchester, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Waters Corporation, Atlas Park, Manchester</wicri:regionArea></affiliation></author><author><name sortKey="Savistchenko, Jimmy" sort="Savistchenko, Jimmy" uniqKey="Savistchenko J" first="Jimmy" last="Savistchenko">Jimmy Savistchenko</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author><author><name sortKey="Vissers, Johannes P C" sort="Vissers, Johannes P C" uniqKey="Vissers J" first="Johannes P. C." last="Vissers">Johannes P. C. Vissers</name><affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Waters Corporation, Atlas Park, Manchester, United Kingdom</addr-line></nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Waters Corporation, Atlas Park, Manchester</wicri:regionArea></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation wicri:level="1"><nlm:aff id="aff1"><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette</wicri:regionArea></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>The aggregation of the baker's yeast prion Sup35p is at the origin of the transmissible [<italic>PSI<sup>+</sup></italic>] trait. We and others have shown that molecular chaperones modulate Sup35p aggregation. However, other protein classes might be involved in [<italic>PSI<sup>+</sup></italic>] formation.</p></sec><sec><title>Results</title><p>We designed a functional proteomic study that combines two techniques to identify modulators of Sup35p aggregation and describe the changes associated to [<italic>PSI<sup>+</sup></italic>] formation. The first allows measuring the effect of fractionated <italic>Saccharomyces cerevisiae</italic> cytosolic extracts from [<italic>PSI<sup>+</sup></italic>] and [<italic>psi<sup>−</sup></italic>] yeast cells on Sup35p assembly. The second is a multiplex qualitative and quantitative comparison of protein composition of active and inactive fractions using a gel-free and label-free LC-MS approach. We identify changes in proteins involved in translation, folding, degradation, oxido-reduction and metabolic processes.</p></sec><sec><title>Conclusion</title><p>Our functional proteomic study provides the first inventory list of over 300 proteins that directly or indirectly affect Sup35p aggregation and [<italic>PSI<sup>+</sup></italic>] formation. Our results highlight the complexity of the cellular changes accompanying [<italic>PSI<sup>+</sup></italic>] formation and pave the way for <italic>in vitro</italic> studies aimed to document the effect of individual and/or combinations of proteins identified here, susceptible of affecting Sup35p assembly.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Prusiner, Sb" uniqKey="Prusiner S">SB Prusiner</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Brundin, P" uniqKey="Brundin P">P Brundin</name></author><author><name sortKey="Melki, R" uniqKey="Melki R">R Melki</name></author><author><name sortKey="Kopito, R" uniqKey="Kopito R">R Kopito</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Castilla, J" uniqKey="Castilla J">J Castilla</name></author><author><name sortKey="Saa, P" uniqKey="Saa P">P Saá</name></author><author><name sortKey="Morales, R" 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<front><journal-meta><journal-id journal-id-type="nlm-ta">PLoS One</journal-id><journal-id journal-id-type="publisher-id">plos</journal-id><journal-id journal-id-type="pmc">plosone</journal-id><journal-title-group><journal-title>PLoS ONE</journal-title></journal-title-group><issn pub-type="epub">1932-6203</issn><publisher><publisher-name>Public Library of Science</publisher-name><publisher-loc>San Francisco, USA</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21931608</article-id><article-id pub-id-type="pmc">3172207</article-id><article-id pub-id-type="publisher-id">PONE-D-11-06726</article-id><article-id pub-id-type="doi">10.1371/journal.pone.0023659</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="Discipline-v2"><subject>Biology</subject><subj-group><subject>Biochemistry</subject><subj-group><subject>Proteins</subject><subj-group><subject>Chaperone Proteins</subject><subject>Protein Interactions</subject><subject>Proteome</subject></subj-group></subj-group></subj-group><subj-group><subject>Biophysics</subject><subj-group><subject>Protein Folding</subject></subj-group></subj-group><subj-group><subject>Proteomics</subject><subj-group><subject>Protein Abundance</subject><subject>Protein Interactions</subject><subject>Spectrometric Identification of Proteins</subject></subj-group></subj-group></subj-group></article-categories><title-group><article-title>Qualitative and Quantitative Multiplexed Proteomic Analysis of Complex Yeast Protein Fractions That Modulate the Assembly of the Yeast Prion Sup35p</article-title><alt-title alt-title-type="running-head">Proteomic Analysis of [<italic>PSI</italic><sup>+</sup>]</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Redeker</surname><given-names>Virginie</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="corresp" rid="cor1"><sup>*</sup></xref></contrib><contrib contrib-type="author"><name><surname>Hughes</surname><given-names>Chris</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Savistchenko</surname><given-names>Jimmy</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Vissers</surname><given-names>Johannes P. C.</given-names></name><xref ref-type="aff" rid="aff2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Melki</surname><given-names>Ronald</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="corresp" rid="cor1"><sup>*</sup></xref></contrib></contrib-group><aff id="aff1"><label>1</label><addr-line>Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France</addr-line></aff><aff id="aff2"><label>2</label><addr-line>Waters Corporation, Atlas Park, Manchester, United Kingdom</addr-line></aff><contrib-group><contrib contrib-type="editor"><name><surname>Zheng</surname><given-names>Jie</given-names></name><role>Editor</role><xref ref-type="aff" rid="edit1"></xref></contrib></contrib-group><aff id="edit1">University of Akron, United States of America</aff><author-notes><corresp id="cor1">* E-mail: <email>redeker@lebs.cnrs-gif.fr</email> (VR); <email>melki@lebs.cnrs-gif.fr</email> (RM)</corresp><fn fn-type="con"><p>Conceived and designed the experiments: VR RM. Performed the experiments: VR JS CH. Analyzed the data: VR JPCV RM. Contributed reagents/materials/analysis tools: JS JPCV. Wrote the paper: VR RM.</p></fn></author-notes><pub-date pub-type="collection"><year>2011</year></pub-date><pub-date pub-type="epub"><day>13</day><month>9</month><year>2011</year></pub-date><volume>6</volume><issue>9</issue><elocation-id>e23659</elocation-id><history><date date-type="received"><day>15</day><month>4</month><year>2011</year></date><date date-type="accepted"><day>22</day><month>7</month><year>2011</year></date></history><permissions><copyright-statement>Redeker et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.</copyright-statement><copyright-year>2011</copyright-year></permissions><abstract><sec><title>Background</title><p>The aggregation of the baker's yeast prion Sup35p is at the origin of the transmissible [<italic>PSI<sup>+</sup></italic>] trait. We and others have shown that molecular chaperones modulate Sup35p aggregation. However, other protein classes might be involved in [<italic>PSI<sup>+</sup></italic>] formation.</p></sec><sec><title>Results</title><p>We designed a functional proteomic study that combines two techniques to identify modulators of Sup35p aggregation and describe the changes associated to [<italic>PSI<sup>+</sup></italic>] formation. The first allows measuring the effect of fractionated <italic>Saccharomyces cerevisiae</italic> cytosolic extracts from [<italic>PSI<sup>+</sup></italic>] and [<italic>psi<sup>−</sup></italic>] yeast cells on Sup35p assembly. The second is a multiplex qualitative and quantitative comparison of protein composition of active and inactive fractions using a gel-free and label-free LC-MS approach. We identify changes in proteins involved in translation, folding, degradation, oxido-reduction and metabolic processes.</p></sec><sec><title>Conclusion</title><p>Our functional proteomic study provides the first inventory list of over 300 proteins that directly or indirectly affect Sup35p aggregation and [<italic>PSI<sup>+</sup></italic>] formation. Our results highlight the complexity of the cellular changes accompanying [<italic>PSI<sup>+</sup></italic>] formation and pave the way for <italic>in vitro</italic> studies aimed to document the effect of individual and/or combinations of proteins identified here, susceptible of affecting Sup35p assembly.</p></sec></abstract><counts><page-count count="11"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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