Title | A new role for Escherichia coli DsbC protein in protection against oxidative stress. |
Publication Type | Journal Article |
Year of Publication | 2014 |
Authors | Denoncin, K., D. Vertommen, I. S. Arts, C. V. Goemans, S. Rahuel-Clermont, J. Messens, and J-F. Collet |
Journal | J Biol Chem |
Volume | 289 |
Issue | 18 |
Pagination | 12356-64 |
Date Published | 2014 May 02 |
ISSN | 1083-351X |
Keywords | Amino 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 |
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. |
DOI | 10.1074/jbc.M114.554055 |
Alternate Journal | J. Biol. Chem. |
PubMed ID | 24634211 |
PubMed Central ID | PMC4007432 |
Grant List | 282335 / / European Research Council / International |
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