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J. Biol. Chem., Vol. 281, Issue 20, 14048-14056, May 19, 2006

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Staphylococcus aureus Operates Protein-tyrosine Phosphorylation through a Specific Mechanism^*

Didier Soulat, Jean-Michel Jault, Bertrand Duclos^¶, Christophe Geourjon^¶, Alain J. Cozzone^¶, and Christophe Grangeasse^¶1

From the ^¶Institute of Biology and Chemistry of Proteins, University of Lyon, CNRS, 69367 Lyon, France, the Laboratory of Molecular and Cellular Biophysics, University of Grenoble, CNRS, CEA, 38054 Grenoble, France, and the Institute of Microbiology and Immunobiology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria

Protein phosphorylation on tyrosine has been originally characterized in animal systems and has been shown to be involved in several fundamental processes including signal transduction, growth control, and malignancy. It has been later demonstrated to occur also in a number of bacteria, and recent data suggest that it may participate in the control of bacterial pathogenicity. In this work, we provide evidence that the Gram-positive human pathogen Staphylococcus aureus harbors a protein-tyrosine kinase activity. This activity is borne by a protein, termed Cap5B2, whose phosphorylating capacity is expressed only in the presence of a stimulatory protein, either Cap5A1 or Cap5A2, that enhances its affinity for the phosphoryl donor ATP. In fact, the last 27/29 amino acids of the C-terminal domain of either polypeptide are sufficient for stimulating Cap5B2 activity. The stimulation of Cap5B2 by Cap5A1 involves essentially three amino acid residues in a helix of Cap5A1 (Asp²⁰², Glu²⁰³, and Asp²⁰⁵) and three residues in a helix (helix 7) of Cap5B2 (Glu¹⁹⁰, Lys¹⁹², and Lys¹⁹³), thus suggesting helix-helix interaction between these two proteins. This type of helix-helix interaction resembles the interaction required for the activation of MinD ATPase by MinE protein in the process of septum-site determination, MinD sharing sequence similarity with Cap5B2. Such activation mechanism is described here in a Gram-positive bacterial tyrosine kinase, and differs from the activation mechanism previously proposed for Gram-negative bacteria. Therefore, it appears that S. aureus, and possibly other Gram-positive bacteria, utilizes a specific molecular mechanism for triggering protein-tyrosine kinase activity.

Received for publication, December 21, 2005 , and in revised form, March 21, 2006.

^* This work was supported by the French Foundation "Vaincre la Mucoviscidose." 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 Table S1 and Figs. S1–S3.

¹ To whom correspondence should be addressed: Institute of Biology and Chemistry of Proteins, 7 passage du Vercors, 69367 Lyon Cedex 07, France. Tel.: 33-4-72-72-26-79; Fax: 33-4-72-72-26-01; E-mail: c.grangeasse{at}ibcp.fr.

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