PhanerochaeteV1, Main, Exploration, bibRecord, 000367

New substrates and activity of Phanerochaete chrysosporium Omega glutathione transferases.

Identifieur interne : 000367 ( Main/Exploration ); précédent : 000366; suivant : 000368

New substrates and activity of Phanerochaete chrysosporium Omega glutathione transferases.

Auteurs : Edgar Meux [France] ; Mélanie Morel ; Tiphaine Lamant ; Philippe Gérardin ; Jean-Pierre Jacquot ; Stéphane Dumarçay ; Eric Gelhaye

Source :

Biochimie [ 1638-6183 ] ; 2013.

RBID : pubmed:23063695

Descripteurs français

English descriptors

KwdEn :
- Catalytic Domain (MeSH), Chromatography, High Pressure Liquid (MeSH), Chromogenic Compounds (MeSH), Cysteine (chemistry), Fagus (chemistry), Fluoresceins (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Immobilized Proteins (chemistry), Immobilized Proteins (genetics), Isoenzymes (chemistry), Isoenzymes (genetics), Kinetics (MeSH), Phanerochaete (chemistry), Phanerochaete (enzymology), Plant Extracts (chemistry), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Sepharose (MeSH), Spectrometry, Fluorescence (MeSH), Substrate Specificity (MeSH), Terpenes (metabolism), Tetralones (metabolism).
MESH :
- chemical , chemistry : Cysteine, Fungal Proteins, Glutathione Transferase, Immobilized Proteins, Isoenzymes, Plant Extracts, Recombinant Proteins.
- chemical , genetics : Fungal Proteins, Glutathione Transferase, Immobilized Proteins, Isoenzymes, Recombinant Proteins.
- chemical , metabolism : Terpenes, Tetralones.
- chemical : Chromogenic Compounds, Fluoresceins, Sepharose.
- chemistry : Fagus, Phanerochaete.
- enzymology : Phanerochaete.
- Catalytic Domain, Chromatography, High Pressure Liquid, Kinetics, Spectrometry, Fluorescence, Substrate Specificity.

Abstract

Omega glutathione transferases (GSTO) constitute a family of proteins with variable distribution throughout living organisms. It is notably expanded in several fungi and particularly in the wood-degrading fungus Phanerochaete chrysosporium, raising questions concerning the function(s) and potential redundancy of these enzymes. Within the fungal families, GSTOs have been poorly studied and their functions remain rather sketchy. In this study, we have used fluorescent compounds as activity reporters to identify putative ligands. Experiments using 5-chloromethylfluorescein diacetate as a tool combined with mass analyses showed that GSTOs are able to cleave ester bonds. Using this property, we developed a specific activity-based profiling method for identifying ligands of PcGSTO3 and PcGSTO4. The results suggest that GSTOs could be involved in the catabolism of toxic compounds like tetralone derivatives. Biochemical investigations demonstrated that these enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteine residue. To access the physiological function of these enzymes and notably during the wood interaction, recombinant proteins have been immobilized on CNBr Sepharose and challenged with beech wood extracts. Coupled with GC-MS experiments this ligand fishing method allowed to identify terpenes as potential substrates of Omega GST suggesting a physiological role during the wood-fungus interactions.

DOI: 10.1016/j.biochi.2012.10.003
PubMed: 23063695

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000398
to stream Main, to step Curation: 000398

Le document en format XML

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<term>Chromatography, High Pressure Liquid (MeSH)</term>
<term>Chromogenic Compounds (MeSH)</term>
<term>Cysteine (chemistry)</term>
<term>Fagus (chemistry)</term>
<term>Fluoresceins (MeSH)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Glutathione Transferase (chemistry)</term>
<term>Glutathione Transferase (genetics)</term>
<term>Immobilized Proteins (chemistry)</term>
<term>Immobilized Proteins (genetics)</term>
<term>Isoenzymes (chemistry)</term>
<term>Isoenzymes (genetics)</term>
<term>Kinetics (MeSH)</term>
<term>Phanerochaete (chemistry)</term>
<term>Phanerochaete (enzymology)</term>
<term>Plant Extracts (chemistry)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Sepharose (MeSH)</term>
<term>Spectrometry, Fluorescence (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Terpenes (metabolism)</term>
<term>Tetralones (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Agarose (MeSH)</term>
<term>Chromatographie en phase liquide à haute performance (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Cystéine (composition chimique)</term>
<term>Dihydro-naphtalénones (métabolisme)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Extraits de plantes (composition chimique)</term>
<term>Fagus (composition chimique)</term>
<term>Fluorescéines (MeSH)</term>
<term>Glutathione transferase (composition chimique)</term>
<term>Glutathione transferase (génétique)</term>
<term>Isoenzymes (composition chimique)</term>
<term>Isoenzymes (génétique)</term>
<term>Phanerochaete (composition chimique)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines immobilisées (composition chimique)</term>
<term>Protéines immobilisées (génétique)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Réactifs chromogènes (MeSH)</term>
<term>Spectrométrie de fluorescence (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Terpènes (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term>
<term>Fungal Proteins</term>
<term>Glutathione Transferase</term>
<term>Immobilized Proteins</term>
<term>Isoenzymes</term>
<term>Plant Extracts</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Glutathione Transferase</term>
<term>Immobilized Proteins</term>
<term>Isoenzymes</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Terpenes</term>
<term>Tetralones</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Chromogenic Compounds</term>
<term>Fluoresceins</term>
<term>Sepharose</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Fagus</term>
<term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term>
<term>Extraits de plantes</term>
<term>Fagus</term>
<term>Glutathione transferase</term>
<term>Isoenzymes</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
<term>Protéines immobilisées</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutathione transferase</term>
<term>Isoenzymes</term>
<term>Protéines fongiques</term>
<term>Protéines immobilisées</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dihydro-naphtalénones</term>
<term>Terpènes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Kinetics</term>
<term>Spectrometry, Fluorescence</term>
<term>Substrate Specificity</term>
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<term>Chromatographie en phase liquide à haute performance</term>
<term>Cinétique</term>
<term>Domaine catalytique</term>
<term>Fluorescéines</term>
<term>Réactifs chromogènes</term>
<term>Spectrométrie de fluorescence</term>
<term>Spécificité du substrat</term>
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<front><div type="abstract" xml:lang="en">Omega glutathione transferases (GSTO) constitute a family of proteins with variable distribution throughout living organisms. It is notably expanded in several fungi and particularly in the wood-degrading fungus Phanerochaete chrysosporium, raising questions concerning the function(s) and potential redundancy of these enzymes. Within the fungal families, GSTOs have been poorly studied and their functions remain rather sketchy. In this study, we have used fluorescent compounds as activity reporters to identify putative ligands. Experiments using 5-chloromethylfluorescein diacetate as a tool combined with mass analyses showed that GSTOs are able to cleave ester bonds. Using this property, we developed a specific activity-based profiling method for identifying ligands of PcGSTO3 and PcGSTO4. The results suggest that GSTOs could be involved in the catabolism of toxic compounds like tetralone derivatives. Biochemical investigations demonstrated that these enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteine residue. To access the physiological function of these enzymes and notably during the wood interaction, recombinant proteins have been immobilized on CNBr Sepharose and challenged with beech wood extracts. Coupled with GC-MS experiments this ligand fishing method allowed to identify terpenes as potential substrates of Omega GST suggesting a physiological role during the wood-fungus interactions.</div>
</front>
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<Month>06</Month>
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<Title>Biochimie</Title>
<ISOAbbreviation>Biochimie</ISOAbbreviation>
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<ArticleTitle>New substrates and activity of Phanerochaete chrysosporium Omega glutathione transferases.</ArticleTitle>
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<Abstract><AbstractText>Omega glutathione transferases (GSTO) constitute a family of proteins with variable distribution throughout living organisms. It is notably expanded in several fungi and particularly in the wood-degrading fungus Phanerochaete chrysosporium, raising questions concerning the function(s) and potential redundancy of these enzymes. Within the fungal families, GSTOs have been poorly studied and their functions remain rather sketchy. In this study, we have used fluorescent compounds as activity reporters to identify putative ligands. Experiments using 5-chloromethylfluorescein diacetate as a tool combined with mass analyses showed that GSTOs are able to cleave ester bonds. Using this property, we developed a specific activity-based profiling method for identifying ligands of PcGSTO3 and PcGSTO4. The results suggest that GSTOs could be involved in the catabolism of toxic compounds like tetralone derivatives. Biochemical investigations demonstrated that these enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteine residue. To access the physiological function of these enzymes and notably during the wood interaction, recombinant proteins have been immobilized on CNBr Sepharose and challenged with beech wood extracts. Coupled with GC-MS experiments this ligand fishing method allowed to identify terpenes as potential substrates of Omega GST suggesting a physiological role during the wood-fungus interactions.</AbstractText>
<CopyrightInformation>Copyright © 2012 Elsevier Masson SAS. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Meux</LastName>
<ForeName>Edgar</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>UMR 1136 INRA-UHP Interactions Arbres/Micro-Organismes, IFR110 Ecosystèmes Forestiers, Agroressources, Bioprocédés et Alimentation, Université de Lorraine, Faculté des Sciences et Technologies, BP 70239, 54506 Vandoeuvre-les-Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Morel</LastName>
<ForeName>Mélanie</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lamant</LastName>
<ForeName>Tiphaine</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gérardin</LastName>
<ForeName>Philippe</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jacquot</LastName>
<ForeName>Jean-Pierre</ForeName>
<Initials>JP</Initials>
</Author>
<Author ValidYN="Y"><LastName>Dumarçay</LastName>
<ForeName>Stéphane</ForeName>
<Initials>S</Initials>
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<MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName>
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<MeshHeading><DescriptorName UI="D005452" MajorTopicYN="N">Fluoresceins</DescriptorName>
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<MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
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<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
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<MeshHeading><DescriptorName UI="D012685" MajorTopicYN="N">Sepharose</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D044024" MajorTopicYN="N">Tetralones</DescriptorName>
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<orgName><li>Université de Lorraine</li>
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<tree><noCountry><name sortKey="Dumarcay, Stephane" sort="Dumarcay, Stephane" uniqKey="Dumarcay S" first="Stéphane" last="Dumarçay">Stéphane Dumarçay</name>
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   |texte=   New substrates and activity of Phanerochaete chrysosporium Omega glutathione transferases.
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New substrates and activity of Phanerochaete chrysosporium Omega glutathione transferases.

New substrates and activity of Phanerochaete chrysosporium Omega glutathione transferases.

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