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Science 326 (5956): 1109-1111

Copyright © 2009 by the American Association for the Advancement of Science

A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation

Matthieu Depuydt,1 Stephen E. Leonard,2 Didier Vertommen,1 Katleen Denoncin,1 Pierre Morsomme,3 Khadija Wahni,4,5 Joris Messens,4,5 Kate S. Carroll,2 Jean-François Collet1,*

Abstract: The thiol group of the amino acid cysteine can be modified to regulate protein activity. The Escherichia coli periplasm is an oxidizing environment in which most cysteine residues are involved in disulfide bonds. However, many periplasmic proteins contain single cysteine residues, which are vulnerable to oxidation to sulfenic acids and then irreversibly modified to sulfinic and sulfonic acids. We discovered that DsbG and DsbC, two thioredoxin-related proteins, control the global sulfenic acid content of the periplasm and protect single cysteine residues from oxidation. DsbG interacts with the YbiS protein and, along with DsbC, regulates oxidation of its catalytic cysteine residue. Thus, a potentially widespread mechanism controls sulfenic acid modification in the cellular environment.

1 de Duve Institute, Université catholique de Louvain, B-1200 Brussels, Belgium.
2 Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109–1048, USA.
3 Institut des Sciences de la Vie, Université catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium.
4 Department of Molecular and Cellular Interactions, Vlaams Instituut voor Biotechnologie (VIB), Vrije Universiteit Brussel, B-1050 Brussels, Belgium.
5 Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.

* To whom correspondence should be addressed. E-mail: jfcollet{at}uclouvain.be

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