Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B |
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Authors: | Vieira Dos Santos Christina Laugier Edith Tarrago Lionel Massot Vincent Issakidis-Bourguet Emmanuelle Rouhier Nicolas Rey Pascal |
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Institution: | CEA, DSV, IBEB, SBVME, Laboratoire d'Ecophysiologie Moléculaire des Plantes (LEMP), UMR 6191, 13108 Saint-Paul-lez-Durance Cedex, France. |
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Abstract: | Methionine sulfoxide reductases (MSRs) A and B reduce methionine sulfoxide (MetSO) S- and R-diastereomers, respectively, back to Met using electrons generally supplied by thioredoxin. The physiological reductants for MSRBs remain unknown in plants, which display a remarkable variety of thioredoxins (Trxs) and glutaredoxins (Grxs). Using recombinant proteins, we show that Arabidopsis plastidial MSRB1 and MSRB2, which differ regarding the number of presumed redox-active cysteines, possess specific reductants. Most simple-module Trxs, especially Trx m1 and Trx y2, are preferential and efficient electron donors towards MSRB2, while the double-module CDSP32 Trx and Grxs can reduce only MSRB1. This study identifies novel types of reductants, related to Grxs and peculiar Trxs, for MSRB proteins displaying only one redox-active cysteine. |
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Keywords: | CDSP32 chloroplastic drought-induced stress protein of 32 kDa Grx glutaredoxin MSR methionine sulfoxide reductase NTRc NADPH-thioredoxin reductase c Trx thioredoxin |
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