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1. Glutathionyl‐hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones

Author

Pierre-Alexandre Lallement, Arnaud Hecker, Claude Didierjean, Frederick Saul, Mélanie Morel-Rouhier, Edgar Meux, Stéphane Dumarçay, Frédérique Favier, José M. Gualberto, Ahmed Haouz, Eric Gelhaye, Nicolas Rouhier, Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire d'Etude et de Recherche sur le Matériau Bois (LERMAB), Université de Lorraine (UL), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), Cristallographie (Plateforme) - Crystallography (Platform), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), ANR as part of the 'Investissements d'Avenir' program (Lab of Excellence ARBRE) [ANR-11-LABX-0002-01], Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Cristallographie (Plate-forme), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Populus trichocarpa, Protein Folding, Plastid, Glutathione transferase, Biophysics, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Growth hormone receptor, Biochemistry, Chloroplast Proteins, Structural Biology, Catalytic Domain, [CHIM.CRIS]Chemical Sciences/Cristallography, Genetics, Nucleoid, Transferase, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, Gene, chemistry.chemical_classification, biology, fungi, Cell Biology, biology.organism_classification, Populus, Enzyme, chemistry, Protein Multimerization, Oxidoreductases, Deglutathionylation, Oxidation-Reduction, Poplar, hormones, hormone substitutes, and hormone antagonists, Cysteine
Abstract

International audience; Glutathionyl-hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt-GHR1 and Pt-GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt-GHR2 localizes in nucleoids. At the structural level, Pt-GHR1 adopts a typical GHR fold, with a dimerization interface comparable to that of the bacterial and fungal GHR counterparts. Pt-GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms.

Published
2014
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2. Sphingobium sp. SYK-6 LigG involved in lignin degradation is structurally and biochemically related to the glutathione transferase omega class

Author

Stéphane Dumarçay, Pascalita Prosper, Mélanie Morel, Guillermo Mulliert, Eiji Masai, Frédérique Favier, Eric Gelhaye, Edgar Meux, Claude Didierjean, Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Dept Bioengn, Nagaoka Univ Technol, Laboratoire d'Etude et de Recherche sur le Matériau Bois (LERMAB), Université de Lorraine (UL), Agence Nationale pour la Recherche [ANR-09-BLAN-0012], Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), and Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL)

Subjects
Models, Molecular, [SDV]Life Sciences [q-bio], Glutathione transferase, BETA-ARYL ETHER, Crystallography, X-Ray, Biochemistry, Lignin, Protein Structure, Secondary, Substrate Specificity, LigG, chemistry.chemical_compound, Structural Biology, Omega class, Transferase, N-CAPPING BOX, Phylogeny, chemistry.chemical_classification, 0303 health sciences, ROLES, biology, Molecular Structure, SUPERFAMILY, Glutathione, CATABOLISM, Isoenzymes, Sphingomonadaceae, ALIGNMENT, Proteobacteria, Protein Binding, Stereochemistry, Biophysics, Thiol transferase, PAUCIMOBILIS SYK-6, 03 medical and health sciences, Bacterial Proteins, Genetics, Cysteine, Binding site, Molecular Biology, 030304 developmental biology, Binding Sites, IDENTIFICATION, STABILITY, 030306 microbiology, Catabolism, CLEAVAGE, Cell Biology, 15. Life on land, biology.organism_classification, Protein Structure, Tertiary, Enzyme, chemistry, Biocatalysis, Mutagenesis, Site-Directed, X-ray structure, Bacteria
Abstract

SpLigG is one of the three glutathione transferases (GSTs) involved in the process of lignin breakdown in the soil bacterium Sphingobium sp. SYK-6. Sequence comparisons showed that SpLigG and several proteobacteria homologues form an independent cluster within cysteine-containing GSTs. The relationship between SpLigG and other GSTs was investigated. The X-ray structure and biochemical properties of SpLigG indicate that this enzyme belongs to the omega class of glutathione transferases. However, the hydrophilic substrate binding site of SpLigG, together with its known ability to stereoselectively deglutathionylate the physiological substrate alpha-glutathionyl-beta-hydroxypropiovanillone, argues for broadening the definition of the omega class. Structured summary of protein interactions: SpLigG and SpLigG bind by X-ray crystallography (View interaction). (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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