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J. Biol. Chem., Vol. 279, Issue 4, 2747-2753, January 23, 2004

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Intracellular Membrane Localization of Pseudomonas ExoS and Yersinia YopE in Mammalian Cells^*

Rebecca Krall, Yue Zhang, and Joseph T. Barbieri

From the Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226

ExoS (453 amino acids) is a bi-functional type-III cytotoxin of Pseudomonas aeruginosa. Residues 96–233 comprise the Rho GTPase-activating protein (Rho GAP) domain, while residues 234–453 comprise the 14-3-3-dependent ADP-ribosyltransferase domain. Residues 51–72 represent a membrane localization domain (MLD), which targets ExoS to perinuclear vesicles within mammalian cells. YopE (219 amino acids) is a type-III cytotoxin of Yersinia that is also a Rho GAP. Residues 96–219 comprise the YopE Rho GAP domain. While the Rho GAP domains of ExoS and YopE share structural homology, unlike ExoS, the intracellular localization of YopE within mammalian cells has not been resolved and is the subject of this investigation. Deletion mapping showed that the N terminus of YopE was required for intracellular membrane localization of YopE in CHO cells. A fusion protein containing the N-terminal 84 amino acids of YopE localized to a punctate-perinuclear region in mammalian cells and co-localized with a fusion protein containing the MLD of ExoS. Residues 54–75 of YopE (termed YopE-MLD) were necessary and sufficient for intracellular localization in mammalian cells. The YopE-MLD localized ExoS to intracellular membranes and targeted ExoS to ADP-ribosylate small molecular weight membrane proteins as observed for native type-III delivered ExoS. These data indicate that the YopE MLD functionally complements the ExoS MLD for intracellular targeting in mammalian cells.

Received for publication, February 25, 2003 , and in revised form, September 12, 2003.

^* This work was supported by grants from the National Institutes of Health and the Cystic Fibrosis Foundation (to J. T. B.). 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.

To whom correspondence should be addressed. Tel.: 414-456-8412; Fax: 414-456-6535; E-mail: jtb01{at}mcw.edu.

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