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

TitleA new role for Escherichia coli DsbC protein in protection against oxidative stress.
Publication TypeJournal Article
Year of Publication2014
AuthorsDenoncin, K., D. Vertommen, I. S. Arts, C. V. Goemans, S. Rahuel-Clermont, J. Messens, and J-F. Collet
JournalJ Biol Chem
Date Published2014 May 02
KeywordsAmino Acid Sequence, Arabinose, Blotting, Western, Carrier Proteins, Cyclohexanones, Cysteine, Disulfides, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Oxidative Stress, Protein Binding, Protein Disulfide-Isomerases, Protein Multimerization, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Substrate Specificity, Sulfenic Acids

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.

Alternate JournalJ. Biol. Chem.
PubMed ID24634211
PubMed Central IDPMC4007432
Grant List282335 / / European Research Council / International
Research group: