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Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor.

Identifieur interne : 000396 ( Main/Exploration ); précédent : 000395; suivant : 000397

Molecular recognition of wood polyphenols by phase II detoxification enzymes of the white rot Trametes versicolor.

Auteurs : Mathieu Schwartz [France] ; Thomas Perrot [France] ; Emmanuel Aubert [France] ; Stéphane Dumarçay [France] ; Frédérique Favier [France] ; Philippe Gérardin [France] ; Mélanie Morel-Rouhier [France] ; Guillermo Mulliert [France] ; Fanny Saiag [France] ; Claude Didierjean [France] ; Eric Gelhaye [France]

Source :

RBID : pubmed:29855494

Descripteurs français

English descriptors

Abstract

Wood decay fungi have complex detoxification systems that enable them to cope with secondary metabolites produced by plants. Although the number of genes encoding for glutathione transferases is especially expanded in lignolytic fungi, little is known about their target molecules. In this study, by combining biochemical, enzymatic and structural approaches, interactions between polyphenols and six glutathione transferases from the white-rot fungus Trametes versicolor have been demonstrated. Two isoforms, named TvGSTO3S and TvGSTO6S have been deeply studied at the structural level. Each isoform shows two distinct ligand-binding sites, a narrow L-site at the dimer interface and a peculiar deep hydrophobic H-site. In TvGSTO3S, the latter appears optimized for aromatic ligand binding such as hydroxybenzophenones. Affinity crystallography revealed that this H-site retains the flavonoid dihydrowogonin from a partially purified wild-cherry extract. Besides, TvGSTO6S binds two molecules of the flavonoid naringenin in the L-site. These data suggest that TvGSTO isoforms could interact with plant polyphenols released during wood degradation.

DOI: 10.1038/s41598-018-26601-3
PubMed: 29855494
PubMed Central: PMC5981210


Affiliations:


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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Benzophenones (chemistry)</term>
<term>Benzophenones (metabolism)</term>
<term>Binding Sites (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Flavonoids (chemistry)</term>
<term>Flavonoids (metabolism)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (metabolism)</term>
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<term>Isoenzymes (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Metabolic Detoxication, Phase II (MeSH)</term>
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<term>Benzophénones (composition chimique)</term>
<term>Benzophénones (métabolisme)</term>
<term>Bois (composition chimique)</term>
<term>Bois (métabolisme)</term>
<term>Cinétique (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Détoxication de phase II (MeSH)</term>
<term>Flavonoïdes (composition chimique)</term>
<term>Flavonoïdes (métabolisme)</term>
<term>Glutathione transferase (composition chimique)</term>
<term>Glutathione transferase (métabolisme)</term>
<term>Isoenzymes (composition chimique)</term>
<term>Isoenzymes (métabolisme)</term>
<term>Polyphénols (composition chimique)</term>
<term>Polyphénols (métabolisme)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Prunus (composition chimique)</term>
<term>Prunus (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
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<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Benzophenones</term>
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<term>Fungal Proteins</term>
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<term>Glutathione transferase</term>
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<term>Protéines fongiques</term>
<term>Prunus</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Prunus</term>
<term>Trametes</term>
<term>Wood</term>
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<term>Benzophénones</term>
<term>Bois</term>
<term>Flavonoïdes</term>
<term>Glutathione transferase</term>
<term>Isoenzymes</term>
<term>Polyphénols</term>
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<term>Trametes</term>
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<term>Binding Sites</term>
<term>Crystallography, X-Ray</term>
<term>Kinetics</term>
<term>Metabolic Detoxication, Phase II</term>
<term>Protein Stability</term>
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<term>Sequence Alignment</term>
<term>Temperature</term>
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<term>Sites de fixation</term>
<term>Stabilité protéique</term>
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<div type="abstract" xml:lang="en">Wood decay fungi have complex detoxification systems that enable them to cope with secondary metabolites produced by plants. Although the number of genes encoding for glutathione transferases is especially expanded in lignolytic fungi, little is known about their target molecules. In this study, by combining biochemical, enzymatic and structural approaches, interactions between polyphenols and six glutathione transferases from the white-rot fungus Trametes versicolor have been demonstrated. Two isoforms, named TvGSTO3S and TvGSTO6S have been deeply studied at the structural level. Each isoform shows two distinct ligand-binding sites, a narrow L-site at the dimer interface and a peculiar deep hydrophobic H-site. In TvGSTO3S, the latter appears optimized for aromatic ligand binding such as hydroxybenzophenones. Affinity crystallography revealed that this H-site retains the flavonoid dihydrowogonin from a partially purified wild-cherry extract. Besides, TvGSTO6S binds two molecules of the flavonoid naringenin in the L-site. These data suggest that TvGSTO isoforms could interact with plant polyphenols released during wood degradation.</div>
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<DateCompleted>
<Year>2019</Year>
<Month>10</Month>
<Day>08</Day>
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<AbstractText>Wood decay fungi have complex detoxification systems that enable them to cope with secondary metabolites produced by plants. Although the number of genes encoding for glutathione transferases is especially expanded in lignolytic fungi, little is known about their target molecules. In this study, by combining biochemical, enzymatic and structural approaches, interactions between polyphenols and six glutathione transferases from the white-rot fungus Trametes versicolor have been demonstrated. Two isoforms, named TvGSTO3S and TvGSTO6S have been deeply studied at the structural level. Each isoform shows two distinct ligand-binding sites, a narrow L-site at the dimer interface and a peculiar deep hydrophobic H-site. In TvGSTO3S, the latter appears optimized for aromatic ligand binding such as hydroxybenzophenones. Affinity crystallography revealed that this H-site retains the flavonoid dihydrowogonin from a partially purified wild-cherry extract. Besides, TvGSTO6S binds two molecules of the flavonoid naringenin in the L-site. These data suggest that TvGSTO isoforms could interact with plant polyphenols released during wood degradation.</AbstractText>
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