Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 20 November 2009:
Vol. 326. no. 5956, pp. 1109 - 1111
DOI: 10.1126/science.1179557
Prev | Table of Contents | Next

Reports

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,*

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

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Disulfide Bond Formation and Cysteine Exclusion in Gram-positive Bacteria.
R. Daniels, P. Mellroth, A. Bernsel, F. Neiers, S. Normark, G. von Heijne, and B. Henriques-Normark (2010)
J. Biol. Chem. 285, 3300-3309
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)