Functional diversification of fungal glutathione transferases from the ure2p class.
Identifieur interne : 000509 ( Main/Exploration ); précédent : 000508; suivant : 000510Functional diversification of fungal glutathione transferases from the ure2p class.
Auteurs : Anne Thuillier [France] ; Andrew A. Ngadin ; Cécile Thion ; Patrick Billard ; Jean-Pierre Jacquot ; Eric Gelhaye ; Mélanie MorelSource :
- International journal of evolutionary biology [ 2090-052X ] ; 2011.
Abstract
The glutathione-S-transferase (GST) proteins represent an extended family involved in detoxification processes. They are divided into various classes with high diversity in various organisms. The Ure2p class is especially expanded in saprophytic fungi compared to other fungi. This class is subdivided into two subclasses named Ure2pA and Ure2pB, which have rapidly diversified among fungal phyla. We have focused our analysis on Basidiomycetes and used Phanerochaete chrysosporium as a model to correlate the sequence diversity with the functional diversity of these glutathione transferases. The results show that among the nine isoforms found in P. chrysosporium, two belonging to Ure2pA subclass are exclusively expressed at the transcriptional level in presence of polycyclic aromatic compounds. Moreover, we have highlighted differential catalytic activities and substrate specificities between Ure2pA and Ure2pB isoforms. This diversity of sequence and function suggests that fungal Ure2p sequences have evolved rapidly in response to environmental constraints.
DOI: 10.4061/2011/938308
PubMed: 22164343
PubMed Central: PMC3227518
Affiliations:
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Ngadin</name></author><author><name sortKey="Thion, Cecile" sort="Thion, Cecile" uniqKey="Thion C" first="Cécile" last="Thion">Cécile Thion</name></author><author><name sortKey="Billard, Patrick" sort="Billard, Patrick" uniqKey="Billard P" first="Patrick" last="Billard">Patrick Billard</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author><author><name sortKey="Morel, Melanie" sort="Morel, Melanie" uniqKey="Morel M" first="Mélanie" last="Morel">Mélanie Morel</name></author></analytic><series><title level="j">International journal of evolutionary biology</title><idno type="eISSN">2090-052X</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The glutathione-S-transferase (GST) proteins represent an extended family involved in detoxification processes. They are divided into various classes with high diversity in various organisms. The Ure2p class is especially expanded in saprophytic fungi compared to other fungi. This class is subdivided into two subclasses named Ure2pA and Ure2pB, which have rapidly diversified among fungal phyla. We have focused our analysis on Basidiomycetes and used Phanerochaete chrysosporium as a model to correlate the sequence diversity with the functional diversity of these glutathione transferases. The results show that among the nine isoforms found in P. chrysosporium, two belonging to Ure2pA subclass are exclusively expressed at the transcriptional level in presence of polycyclic aromatic compounds. Moreover, we have highlighted differential catalytic activities and substrate specificities between Ure2pA and Ure2pB isoforms. This diversity of sequence and function suggests that fungal Ure2p sequences have evolved rapidly in response to environmental constraints.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">22164343</PMID><DateCompleted><Year>2012</Year><Month>08</Month><Day>23</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2090-052X</ISSN><JournalIssue CitedMedium="Internet"><Volume>2011</Volume><PubDate><Year>2011</Year></PubDate></JournalIssue><Title>International journal of evolutionary biology</Title><ISOAbbreviation>Int J Evol Biol</ISOAbbreviation></Journal><ArticleTitle>Functional diversification of fungal glutathione transferases from the ure2p class.</ArticleTitle><Pagination><MedlinePgn>938308</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4061/2011/938308</ELocationID><Abstract><AbstractText>The glutathione-S-transferase (GST) proteins represent an extended family involved in detoxification processes. They are divided into various classes with high diversity in various organisms. The Ure2p class is especially expanded in saprophytic fungi compared to other fungi. This class is subdivided into two subclasses named Ure2pA and Ure2pB, which have rapidly diversified among fungal phyla. We have focused our analysis on Basidiomycetes and used Phanerochaete chrysosporium as a model to correlate the sequence diversity with the functional diversity of these glutathione transferases. The results show that among the nine isoforms found in P. chrysosporium, two belonging to Ure2pA subclass are exclusively expressed at the transcriptional level in presence of polycyclic aromatic compounds. Moreover, we have highlighted differential catalytic activities and substrate specificities between Ure2pA and Ure2pB isoforms. This diversity of sequence and function suggests that fungal Ure2p sequences have evolved rapidly in response to environmental constraints.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Thuillier</LastName><ForeName>Anne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherches INRA UHP 1136 Interaction Arbres Microorganismes, IFR 110 Ecosystèmes Forestiers, Agroressources, Bioprocédés et Alimentation, Faculté des Sciences et Technologies, Nancy Université BP 70239, 54506 Vandoeuvre-lès-Nancy Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ngadin</LastName><ForeName>Andrew A</ForeName><Initials>AA</Initials></Author><Author ValidYN="Y"><LastName>Thion</LastName><ForeName>Cécile</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Billard</LastName><ForeName>Patrick</ForeName><Initials>P</Initials></Author><Author 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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>Vandœuvre-lès-Nancy</li></settlement></list><tree><noCountry><name sortKey="Billard, Patrick" sort="Billard, Patrick" uniqKey="Billard P" first="Patrick" last="Billard">Patrick Billard</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</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, Melanie" sort="Morel, Melanie" uniqKey="Morel M" first="Mélanie" last="Morel">Mélanie Morel</name><name sortKey="Ngadin, Andrew A" sort="Ngadin, Andrew A" uniqKey="Ngadin A" first="Andrew A" last="Ngadin">Andrew A. Ngadin</name><name sortKey="Thion, Cecile" sort="Thion, Cecile" uniqKey="Thion C" first="Cécile" last="Thion">Cécile Thion</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Thuillier, Anne" sort="Thuillier, Anne" uniqKey="Thuillier A" first="Anne" last="Thuillier">Anne Thuillier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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