| Literature DB >> 25455804 |
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.Entities:
Keywords: Deglutathionylation; Glutathione transferase; Plastid; Poplar
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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