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

被引:86
作者
Dos Santos, Christina Vieira [1 ]
Laugier, Edith [1 ]
Tarrago, Lionel [1 ]
Massot, Vincent [2 ]
Issakidis-Bourguet, Emmanuelle [2 ]
Rouhier, Nicolas [3 ]
Rey, Pascal [1 ]
机构
[1] CEA, DSV,IBEB, SBVME,UMR 6191, Lab Ecophysiol Mol Plant, F-13108 St Paul Les Durance, France
[2] Univ Paris 11, Ctr Natl Rech Sci, Inst Biotechnol Plant, Unit Mix Rech 8618, F-91405 Orsay, France
[3] Univ Nancy 1, INRA 1136, IFR,GEEF 110,Fac Sci, Unite Mixte Rech,Interact Arbres Microorganismes, F-54506 Vandoeuvre Les Nancy, France
关键词
glutaredoxin; chloroplast; methionine; methionine sulfoxide reductase; plant; thioredoxin;
D O I
10.1016/j.febslet.2007.07.081
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Methionine suffoxide 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 doublemodule 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 redoxactive cysteine. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:4371 / 4376
页数:6
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