Characterization of a Phanerochaete chrysosporium glutathione transferase reveals a novel structural and functional class with ligandin properties.
Identifieur interne : 000885 ( Main/Exploration ); précédent : 000884; suivant : 000886Characterization of a Phanerochaete chrysosporium glutathione transferase reveals a novel structural and functional class with ligandin properties.
Auteurs : Yann Mathieu [France] ; Pascalita Prosper ; Marc Buée ; Stéphane Dumarçay ; Frédérique Favier ; Eric Gelhaye ; Philippe Gérardin ; Luc Harvengt ; Jean-Pierre Jacquot ; Tiphaine Lamant ; Edgar Meux ; Sandrine Mathiot ; Claude Didierjean ; Mélanie MorelSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2012.
Descripteurs français
- KwdFr :
- Anilino-naphtalènesulfonates (pharmacologie), Biotechnologie (méthodes), Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (méthodes), Données de séquences moléculaires (MeSH), Fixation compétitive (MeSH), Glutathion (composition chimique), Glutathione transferase (composition chimique), Glutathione transferase (métabolisme), Isoformes de protéines (MeSH), Liaison aux protéines (MeSH), Lignine (MeSH), Phanerochaete (métabolisme), Protéines recombinantes (composition chimique), Sites de fixation (MeSH), Spectrométrie de masse (méthodes).
- MESH :
- composition chimique : Glutathion, Glutathione transferase, Protéines recombinantes.
- métabolisme : Glutathione transferase, Phanerochaete.
- méthodes : Biotechnologie, Cristallographie aux rayons X, Spectrométrie de masse.
- pharmacologie : Anilino-naphtalènesulfonates.
- Clonage moléculaire, Conformation des protéines, Données de séquences moléculaires, Fixation compétitive, Isoformes de protéines, Liaison aux protéines, Lignine, Sites de fixation.
English descriptors
- KwdEn :
- Anilino Naphthalenesulfonates (pharmacology), Binding Sites (MeSH), Binding, Competitive (MeSH), Biotechnology (methods), Cloning, Molecular (MeSH), Crystallography, X-Ray (methods), Glutathione (chemistry), Glutathione Transferase (chemistry), Glutathione Transferase (metabolism), Lignin (MeSH), Mass Spectrometry (methods), Molecular Sequence Data (MeSH), Phanerochaete (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Protein Isoforms (MeSH), Recombinant Proteins (chemistry).
- MESH :
- chemical , chemistry : Glutathione, Glutathione Transferase, Recombinant Proteins.
- chemical , metabolism : Glutathione Transferase.
- chemical , pharmacology : Anilino Naphthalenesulfonates.
- metabolism : Phanerochaete.
- methods : Biotechnology, Crystallography, X-Ray, Mass Spectrometry.
- Binding Sites, Binding, Competitive, Cloning, Molecular, Lignin, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Isoforms.
Abstract
Glutathione S-transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. A new fungal specific class of GST has been highlighted by genomic approaches. The biochemical and structural characterization of one isoform of this class in Phanerochaete chrysosporium revealed original properties. The three-dimensional structure showed a new dimerization mode and specific features by comparison with the canonical GST structure. An additional β-hairpin motif in the N-terminal domain prevents the formation of the regular GST dimer and acts as a lid, which closes upon glutathione binding. Moreover, this isoform is the first described GST that contains all secondary structural elements, including helix α4' in the C-terminal domain, of the presumed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2). A sulfate binding site has been identified close to the glutathione binding site and allows the binding of 8-anilino-1-naphtalene sulfonic acid. Competition experiments between 8-anilino-1-naphtalene sulfonic acid, which has fluorescent properties, and various molecules showed that this GST binds glutathionylated and sulfated compounds but also wood extractive molecules, such as vanillin, chloronitrobenzoic acid, hydroxyacetophenone, catechins, and aldehydes, in the glutathione pocket. This enzyme could thus function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it could also act as a ligandin of wood extractive compounds. These new structural and functional properties lead us to propose that this GST belongs to a new class that we name GSTFuA, for fungal specific GST class A.
DOI: 10.1074/jbc.M112.402776
PubMed: 23007392
PubMed Central: PMC3493941
Affiliations:
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X-Ray (methods)</term><term>Glutathione (chemistry)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (metabolism)</term><term>Lignin (MeSH)</term><term>Mass Spectrometry (methods)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Isoforms (MeSH)</term><term>Recombinant Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anilino-naphtalènesulfonates (pharmacologie)</term><term>Biotechnologie (méthodes)</term><term>Clonage moléculaire (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (méthodes)</term><term>Données de séquences moléculaires (MeSH)</term><term>Fixation compétitive (MeSH)</term><term>Glutathion (composition chimique)</term><term>Glutathione transferase (composition chimique)</term><term>Glutathione transferase 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moléculaire</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Fixation compétitive</term><term>Isoformes de protéines</term><term>Liaison aux protéines</term><term>Lignine</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione S-transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. A new fungal specific class of GST has been highlighted by genomic approaches. The biochemical and structural characterization of one isoform of this class in Phanerochaete chrysosporium revealed original properties. The three-dimensional structure showed a new dimerization mode and specific features by comparison with the canonical GST structure. An additional β-hairpin motif in the N-terminal domain prevents the formation of the regular GST dimer and acts as a lid, which closes upon glutathione binding. Moreover, this isoform is the first described GST that contains all secondary structural elements, including helix α4' in the C-terminal domain, of the presumed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2). A sulfate binding site has been identified close to the glutathione binding site and allows the binding of 8-anilino-1-naphtalene sulfonic acid. Competition experiments between 8-anilino-1-naphtalene sulfonic acid, which has fluorescent properties, and various molecules showed that this GST binds glutathionylated and sulfated compounds but also wood extractive molecules, such as vanillin, chloronitrobenzoic acid, hydroxyacetophenone, catechins, and aldehydes, in the glutathione pocket. This enzyme could thus function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it could also act as a ligandin of wood extractive compounds. These new structural and functional properties lead us to propose that this GST belongs to a new class that we name GSTFuA, for fungal specific GST class A.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23007392</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>31</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>287</Volume><Issue>46</Issue><PubDate><Year>2012</Year><Month>Nov</Month><Day>09</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Characterization of a Phanerochaete chrysosporium glutathione transferase reveals a novel structural and functional class with ligandin properties.</ArticleTitle><Pagination><MedlinePgn>39001-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M112.402776</ELocationID><Abstract><AbstractText>Glutathione S-transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. A new fungal specific class of GST has been highlighted by genomic approaches. The biochemical and structural characterization of one isoform of this class in Phanerochaete chrysosporium revealed original properties. The three-dimensional structure showed a new dimerization mode and specific features by comparison with the canonical GST structure. An additional β-hairpin motif in the N-terminal domain prevents the formation of the regular GST dimer and acts as a lid, which closes upon glutathione binding. Moreover, this isoform is the first described GST that contains all secondary structural elements, including helix α4' in the C-terminal domain, of the presumed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2). A sulfate binding site has been identified close to the glutathione binding site and allows the binding of 8-anilino-1-naphtalene sulfonic acid. Competition experiments between 8-anilino-1-naphtalene sulfonic acid, which has fluorescent properties, and various molecules showed that this GST binds glutathionylated and sulfated compounds but also wood extractive molecules, such as vanillin, chloronitrobenzoic acid, hydroxyacetophenone, catechins, and aldehydes, in the glutathione pocket. This enzyme could thus function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it could also act as a ligandin of wood extractive compounds. These new structural and functional properties lead us to propose that this GST belongs to a new class that we name GSTFuA, for fungal specific GST class A.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mathieu</LastName><ForeName>Yann</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbre-Microorganismes, UMR 1136, Institut Fédératif de Recherche 110 EFABA, Vandoeuvre-lès-Nancy F-54506, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prosper</LastName><ForeName>Pascalita</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Buée</LastName><ForeName>Marc</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Dumarçay</LastName><ForeName>Stéphane</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Favier</LastName><ForeName>Frédérique</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Gérardin</LastName><ForeName>Philippe</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Harvengt</LastName><ForeName>Luc</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Lamant</LastName><ForeName>Tiphaine</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Meux</LastName><ForeName>Edgar</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Mathiot</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials></Author><Author 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first="Stéphane" last="Dumarçay">Stéphane Dumarçay</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="Gerardin, Philippe" sort="Gerardin, Philippe" uniqKey="Gerardin P" first="Philippe" last="Gérardin">Philippe Gérardin</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="Lamant, Tiphaine" sort="Lamant, Tiphaine" uniqKey="Lamant T" first="Tiphaine" last="Lamant">Tiphaine Lamant</name><name sortKey="Mathiot, Sandrine" sort="Mathiot, Sandrine" uniqKey="Mathiot S" first="Sandrine" last="Mathiot">Sandrine Mathiot</name><name sortKey="Meux, Edgar" sort="Meux, Edgar" uniqKey="Meux E" first="Edgar" last="Meux">Edgar Meux</name><name sortKey="Morel, Melanie" sort="Morel, Melanie" uniqKey="Morel M" first="Mélanie" last="Morel">Mélanie Morel</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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