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Glutathionyl‐hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones
Author(s) -
Lallement PierreAlexandre,
Meux Edgar,
Gualberto José M.,
Dumarcay Stéphane,
Favier Frédérique,
Didierjean Claude,
Saul Frederick,
Haouz Ahmed,
Morel-Rouhier Mélanie,
Gelhaye Eric,
Rouhier Nicolas,
Hecker Arnaud
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.021
Subject(s) - hydroquinone , biochemistry , chemistry , cysteine , plastid , enzyme , biology , chloroplast , gene
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.