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J. Biol. Chem., Vol. 280, Issue 46, 38682-38688, November 18, 2005

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Recognition and Ubiquitination of Salmonella Type III Effector SopA by a Ubiquitin E3 Ligase, HsRMA1^*

From the Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907

Salmonella translocate bacterial effectors into host cells to confer bacterial entry and survival. It is not known how the host cells cope with the influx of these effectors. We report here that the Salmonella effector, SopA, interacts with host HsRMA1, a ubiquitin E3 ligase with a previously unknown function. SopA is ubiquitinated and degraded by the HsRMA1-mediated ubiquitination pathway. A sopA mutant escapes out of the Salmonella-containing vacuoles less frequently to the cytosol than wild type Salmonella in HeLa cells in a HsRMA1-dependent manner. Our data suggest that efficient bacterial escape into the cytosol of epithelial cells requires HsRMA1-mediated SopA ubiquitination and contributes to Salmonella-induced enteropathogenicity.

Received for publication, June 9, 2005 , and in revised form, August 24, 2005.

^* This research was supported by National Institutes of Health Grant AI49978 (to D. Z.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Both authors contributed equally.

² To whom correspondence should be addressed. Tel.: 765-494-8159; Fax: 765-494-0876; E-mail: zhoud{at}purdue.edu.

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