Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B

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...

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Published in:FEBS letters 2007-09, Vol.581 (23), p.4371-4376
Main Authors: Vieira Dos Santos, Christina, Laugier, Edith, Tarrago, Lionel, Massot, Vincent, Issakidis-Bourguet, Emmanuelle, Rouhier, Nicolas, Rey, Pascal
Format: Article
Language:English
Subjects:
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Biochemistry, Molecular Biology
CDSP32
Chloroplast
chloroplastic drought-induced stress protein of 32 kDa
Cysteine - genetics
Cysteine - metabolism
Electron Transport
Glutaredoxin
Glutaredoxins - genetics
Glutaredoxins - metabolism
Grx
Life Sciences
Methionine
Methionine sulfoxide reductase
Methionine Sulfoxide Reductases
MSR
Mutagenesis, Site-Directed
NADPH-thioredoxin reductase c
NTRc
Oxidation-Reduction
Oxidoreductases - genetics
Oxidoreductases - metabolism
Plant
Plastids - enzymology
Plastids - metabolism
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Substrate Specificity
Thioredoxin
Thioredoxins - genetics
Thioredoxins - metabolism
Time Factors
Trx
Vegetal Biology
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.07.081