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

Pierre-Alexandre Lallement, Edgar Meux, José M Gualberto, Stéphane Dumarcay, Frédérique Favier, Claude Didierjean, Frederick Saul, Ahmed Haouz, Mélanie Morel-Rouhier, Eric Gelhaye, Nicolas Rouhier, Arnaud Hecker

Index: FEBS Lett. 589(1) , 37-44, (2014)

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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.