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

Denoncin, Katleen;Vertommen, Didier;Arts, Isabelle;Goemans, Camille;Collet, Jean-François
(2014) Journal of Biological Chemistry — Vol. 289, n° 18, p. 12356-12364 (2014)

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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.
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Denoncin, K., Vertommen, D., Arts, I., Goemans, C., & Collet, J.-F. (2014). A new role for Escherichia coli DsbC protein in protection against oxidative stress. Journal of Biological Chemistry, 289(18), 12356-12364. https://doi.org/10.1074/jbc.M114.554055 (Original work published 2014)