|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|
|Date Published||2014 May 02|
|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|
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 Journal||J. Biol. Chem.|
|PubMed Central ID||PMC4007432|
|Grant List||282335 / / European Research Council / International|
A new role for Escherichia coli DsbC protein in protection against oxidative stress.