Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.
Identifieur interne : 000375 ( Main/Exploration ); précédent : 000374; suivant : 000376Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.
Auteurs : Yann Mathieu [France] ; Pascalita Prosper ; Frédérique Favier ; Luc Harvengt ; Claude Didierjean ; Jean-Pierre Jacquot ; Mélanie Morel-Rouhier ; Eric GelhayeSource :
- PloS one [ 1932-6203 ] ; 2013.
Descripteurs français
- KwdFr :
- Amorces ADN (MeSH), Clonage moléculaire (MeSH), Coprinus (enzymologie), Cristallisation (MeSH), Données de séquences moléculaires (MeSH), Glutathione transferase (composition chimique), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Modèles moléculaires (MeSH), Phanerochaete (enzymologie), Similitude de séquences d'acides aminés (MeSH), Spectrométrie de fluorescence (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Glutathione transferase.
- enzymologie : Coprinus, Phanerochaete.
- génétique : Glutathione transferase.
- métabolisme : Glutathione transferase.
- Amorces ADN, Clonage moléculaire, Cristallisation, Données de séquences moléculaires, Modèles moléculaires, Similitude de séquences d'acides aminés, Spectrométrie de fluorescence, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Coprinus (enzymology), Crystallization (MeSH), DNA Primers (MeSH), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Sequence Homology, Amino Acid (MeSH), Spectrometry, Fluorescence (MeSH).
- MESH :
- chemical , chemistry : Glutathione Transferase.
- chemical , genetics : Glutathione Transferase.
- chemical , metabolism : Glutathione Transferase.
- chemical : DNA Primers.
- enzymology : Coprinus, Phanerochaete.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Crystallization, Models, Molecular, Molecular Sequence Data, Sequence Homology, Amino Acid, Spectrometry, Fluorescence.
Abstract
Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry.
DOI: 10.1371/journal.pone.0080298
PubMed: 24278272
PubMed Central: PMC3835915
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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transferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Crystallization</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term><term>Spectrometry, Fluorescence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Clonage moléculaire</term><term>Cristallisation</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Similitude de séquences d'acides aminés</term><term>Spectrométrie de fluorescence</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24278272</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><Issue>11</Issue><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.</ArticleTitle><Pagination><MedlinePgn>e80298</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0080298</ELocationID><Abstract><AbstractText>Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mathieu</LastName><ForeName>Yann</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Université de Lorraine, IAM, UMR 1136, IFR 110 EFABA, Vandoeuvre-les-Nancy, France ; INRA, IAM, UMR 1136, Champenoux, France ; Laboratoire de biotechnologie, Pôle Biotechnologie et Sylviculture Avancée, FCBA, Campus Forêt-Bois de Pierroton, Cestas, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prosper</LastName><ForeName>Pascalita</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Favier</LastName><ForeName>Frédérique</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Harvengt</LastName><ForeName>Luc</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Morel-Rouhier</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></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>2013</Year><Month>11</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS 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Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>07</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>10</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>9</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24278272</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0080298</ArticleId><ArticleId 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IdType="pubmed">18845158</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Metz</li><li>Nancy</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><noCountry><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><name sortKey="Favier, Frederique" sort="Favier, Frederique" uniqKey="Favier F" first="Frédérique" last="Favier">Frédérique Favier</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Harvengt, Luc" sort="Harvengt, Luc" uniqKey="Harvengt L" first="Luc" last="Harvengt">Luc Harvengt</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><name sortKey="Prosper, Pascalita" sort="Prosper, Pascalita" uniqKey="Prosper P" first="Pascalita" last="Prosper">Pascalita Prosper</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Mathieu, Yann" sort="Mathieu, Yann" uniqKey="Mathieu Y" first="Yann" last="Mathieu">Yann Mathieu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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