Literature DB >> 25455804

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

Pierre-Alexandre Lallement1, Edgar Meux1, José M Gualberto2, Stéphane Dumarcay3, Frédérique Favier4, Claude Didierjean4, Frederick Saul5, Ahmed Haouz5, Mélanie Morel-Rouhier1, Eric Gelhaye1, Nicolas Rouhier1, Arnaud Hecker6.   

Abstract

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.
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Deglutathionylation; Glutathione transferase; Plastid; Poplar

Mesh:

Substances:

Year:  2014        PMID: 25455804     DOI: 10.1016/j.febslet.2014.11.021

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  9 in total

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2.  Genome-wide identification and characterization of glutathione S-transferase gene family in Musa acuminata L. AAA group and gaining an insight to their role in banana fruit development.

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4.  The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1.

Authors:  Henri Pégeot; Cha San Koh; Benjamin Petre; Sandrine Mathiot; Sébastien Duplessis; Arnaud Hecker; Claude Didierjean; Nicolas Rouhier
Journal:  Front Plant Sci       Date:  2014-12-23       Impact factor: 5.753

5.  Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.

Authors:  Mathieu Schwartz; Claude Didierjean; Arnaud Hecker; Jean-Michel Girardet; Mélanie Morel-Rouhier; Eric Gelhaye; Frédérique Favier
Journal:  PLoS One       Date:  2016-10-13       Impact factor: 3.240

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Review 7.  Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.

Authors:  Elodie Sylvestre-Gonon; Simon R Law; Mathieu Schwartz; Kevin Robe; Olivier Keech; Claude Didierjean; Christian Dubos; Nicolas Rouhier; Arnaud Hecker
Journal:  Front Plant Sci       Date:  2019-05-22       Impact factor: 5.753

8.  Structural Characterization of the Xi Class Glutathione Transferase From the Haloalkaliphilic Archaeon Natrialba magadii.

Authors:  Adele Di Matteo; Luca Federici; Michele Masulli; Erminia Carletti; Daniele Santorelli; Jennifer Cassidy; Francesca Paradisi; Carmine Di Ilio; Nerino Allocati
Journal:  Front Microbiol       Date:  2019-01-18       Impact factor: 5.640

9.  Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress.

Authors:  Meiru Si; Chengchuan Che; Guanxi Li; Xiaona Li; Zhijin Gong; Jinfeng Liu; Ge Yang; Can Chen
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  9 in total

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