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ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.
Nature. 2003 Oct 30; 425(6961):980-4.Nat

Abstract

Proteins contain thiol-bearing cysteine residues that are sensitive to oxidation, and this may interfere with biological function either as 'damage' or in the context of oxidant-dependent signal transduction. Cysteine thiols oxidized to sulphenic acid are generally unstable, either forming a disulphide with a nearby thiol or being further oxidized to a stable sulphinic acid. Cysteine-sulphenic acids and disulphides are known to be reduced by glutathione or thioredoxin in biological systems, but cysteine-sulphinic acid derivatives have been viewed as irreversible protein modifications. Here we identify a yeast protein of relative molecular mass M(r) = 13,000, which we have named sulphiredoxin (identified by the US spelling 'sulfiredoxin', in the Saccharomyces Genome Database), that is conserved in higher eukaryotes and reduces cysteine-sulphinic acid in the yeast peroxiredoxin Tsa1. Peroxiredoxins are ubiquitous thiol-containing antioxidants that reduce hydroperoxides and control hydroperoxide-mediated signalling in mammals. The reduction reaction catalysed by sulphiredoxin requires ATP hydrolysis and magnesium, involving a conserved active-site cysteine residue which forms a transient disulphide linkage with Tsa1. We propose that reduction of cysteine-sulphinic acids by sulphiredoxin involves activation by phosphorylation followed by a thiol-mediated reduction step. Sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine-sulphinic acid modifications, and in signalling pathways involving protein oxidation.

Authors+Show Affiliations

Laboratoire Stress Oxydants et Cancer, SBGM, DBJC, CEA-Saclay, 91191 Gif-sur-Yvette cedex, France.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

14586471

Citation

Biteau, Benoît, et al. "ATP-dependent Reduction of Cysteine-sulphinic Acid By S. Cerevisiae Sulphiredoxin." Nature, vol. 425, no. 6961, 2003, pp. 980-4.
Biteau B, Labarre J, Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature. 2003;425(6961):980-4.
Biteau, B., Labarre, J., & Toledano, M. B. (2003). ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature, 425(6961), 980-4.
Biteau B, Labarre J, Toledano MB. ATP-dependent Reduction of Cysteine-sulphinic Acid By S. Cerevisiae Sulphiredoxin. Nature. 2003 Oct 30;425(6961):980-4. PubMed PMID: 14586471.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. AU - Biteau,Benoît, AU - Labarre,Jean, AU - Toledano,Michel B, PY - 2003/06/23/received PY - 2003/09/08/accepted PY - 2003/10/31/pubmed PY - 2003/12/10/medline PY - 2003/10/31/entrez SP - 980 EP - 4 JF - Nature JO - Nature VL - 425 IS - 6961 N2 - Proteins contain thiol-bearing cysteine residues that are sensitive to oxidation, and this may interfere with biological function either as 'damage' or in the context of oxidant-dependent signal transduction. Cysteine thiols oxidized to sulphenic acid are generally unstable, either forming a disulphide with a nearby thiol or being further oxidized to a stable sulphinic acid. Cysteine-sulphenic acids and disulphides are known to be reduced by glutathione or thioredoxin in biological systems, but cysteine-sulphinic acid derivatives have been viewed as irreversible protein modifications. Here we identify a yeast protein of relative molecular mass M(r) = 13,000, which we have named sulphiredoxin (identified by the US spelling 'sulfiredoxin', in the Saccharomyces Genome Database), that is conserved in higher eukaryotes and reduces cysteine-sulphinic acid in the yeast peroxiredoxin Tsa1. Peroxiredoxins are ubiquitous thiol-containing antioxidants that reduce hydroperoxides and control hydroperoxide-mediated signalling in mammals. The reduction reaction catalysed by sulphiredoxin requires ATP hydrolysis and magnesium, involving a conserved active-site cysteine residue which forms a transient disulphide linkage with Tsa1. We propose that reduction of cysteine-sulphinic acids by sulphiredoxin involves activation by phosphorylation followed by a thiol-mediated reduction step. Sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine-sulphinic acid modifications, and in signalling pathways involving protein oxidation. SN - 1476-4687 UR - https://www.unboundmedicine.com/medline/citation/14586471/ATP_dependent_reduction_of_cysteine_sulphinic_acid_by_S__cerevisiae_sulphiredoxin_ L2 - https://doi.org/10.1038/nature02075 DB - PRIME DP - Unbound Medicine ER -