Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones - Université de Lorraine
Article Dans Une Revue FEBS Letters Année : 2015

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

Pierre-Alexandre Lallement
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Edgar Meux
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Éric Gelhaye
Nicolas Rouhier
Arnaud Hecker

Résumé

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.
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Dates et versions

hal-01522015 , version 1 (12-05-2017)

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Citer

Pierre-Alexandre Lallement, Edgar Meux, José M. Gualberto, Stéphane Dumarcay, Frédérique Favier, et al.. Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones. FEBS Letters, 2015, 589 (1), pp.37 - 44. ⟨10.1016/j.febslet.2014.11.021⟩. ⟨hal-01522015⟩
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