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

Katleen Denoncin, Didier Vertommen, Isabelle S Arts, Camille V Goemans, Sophie Rahuel-Clermont, Joris Messens, Jean-François Collet

The Journal of biological chemistry 2014 May 02

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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.

Citation

Katleen Denoncin, Didier Vertommen, Isabelle S Arts, Camille V Goemans, Sophie Rahuel-Clermont, Joris Messens, Jean-François Collet. A new role for Escherichia coli DsbC protein in protection against oxidative stress. The Journal of biological chemistry. 2014 May 02;289(18):12356-64