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J Biol Chem. 2014 May 2;289(18):12356-64. doi: 10.1074/jbc.M114.554055. Epub 2014 Mar 14.

A new role for Escherichia coli DsbC protein in protection against oxidative stress.

Author information

1
From the de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.

Abstract

We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm. We found that DsbC regulates the redox state of the single cysteine of the L-arabinose-binding protein AraF. This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-linked homodimer under oxidative stress conditions, preventing L-arabinose binding. DsbC, unlike the homologous protein DsbG, reduces the intermolecular disulfide, restoring AraF binding properties. Thus, our results reveal a new link between oxidative protein folding and the defense mechanisms against oxidative stress.

KEYWORDS:

Disulfide; DsbC; Escherichia coli; Oxidative Stress; Protein Folding; Redox Regulation; Sulfenic Acid; Thioredoxin

PMID:
24634211
PMCID:
PMC4007432
DOI:
10.1074/jbc.M114.554055
[Indexed for MEDLINE]
Free PMC Article

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