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J. Biol. Chem., Vol. 280, Issue 1, 156-163, January 7, 2005

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Modulation of Yersinia Type Three Secretion System by the S1 Domain of Polynucleotide Phosphorylase^*

Jason A. Rosenzweig, Gabriela Weltman, Gregory V. Plano, and Kurt Schesser

From the Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, Florida 33101

Both low temperatures and encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. Previous work has shown that the exoribonuclease polynucleotide phosphorylase (PNPase) is required for Yersiniae to grow at low temperatures. Here, we show that PNPase also enhances the ability of Yersinia pseudotuberculosis and Yersinia pestis to withstand the killing activities of murine macrophages. PNPase is required for the optimal functioning of the Yersinia type three secretion system (TTSS), an organelle that injects effector proteins directly into host cells. Unexpectedly, the effect of PNPase on the TTSS is independent of its ribonuclease activity and instead requires its S1 RNA binding domain. In contrast, catalytically inactive enzyme does not enhance the low temperature growth effect of PNPase. Surprisingly, wild-type-like TTSS functioning was restored to the pnp mutant strain by expressing just the 70 amino acid S1 domains from either PNPase, RNase R, RNase II, or RpsA. Our findings suggest that PNPase plays multifaceted roles in enhancing Yersinia survival in response to stressful conditions.

Received for publication, May 20, 2004 , and in revised form, October 14, 2004.

^* This work was supported by the Glaser Foundation (Miami, FL), the Department of Microbiology and Immunology, University of Miami School of Medicine, and Public Health Service Grants R01 AI53459 (to K. S.) and AI50552 (to G. V. P.) from the NIAID, National Institutes of Health. 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.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Materials.

To whom correspondence should be addressed: Dept. of Microbiology and Immunology, University of Miami School of Medicine, P. O. Box 016960 (R-138) Miami, FL 33101. Tel.: 305-243-4760; Fax: 305-243-4623; E-mail: kschesser{at}med.miami.edu.

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