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Originally published In Press as doi:10.1074/jbc.M110880200 on December 20, 2001

J. Biol. Chem., Vol. 277, Issue 9, 7127-7135, March 1, 2002
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Tyrosine Phosphorylation of Protein Kinase Wzc from Escherichia coli K12 Occurs through a Two-step Process*

Christophe Grangeasse, Patricia Doublet, and Alain J. CozzoneDagger

From the Institut de Biologie et Chimie des Protéines, CNRS, Université de Lyon, 7 passage du Vercors, Lyon 69367, cedex 07, France

In bacteria, several proteins have been shown to autophosphorylate on tyrosine residues, but little is known on the molecular mechanism of this modification. To get more information on this matter, we have analyzed in detail the phosphorylation of a particular autokinase, protein Wzc, from Escherichia coli K12. The analysis of the hydropathic profile of this protein indicates that it is composed of two main domains: an N-terminal domain, including two transmembrane alpha -helices, and a C-terminal cytoplasmic domain. The C-terminal domain alone can undergo autophosphorylation and thus appears to harbor the protein-tyrosine kinase activity. By contrast, the N-terminal domain is not phosphorylated when incubated either alone or in the presence of the C-domain, and does not influence the extent of phosphorylation of the C-domain. The C-domain contains six different sites of phosphorylation. Among these, five are located at the C-terminal end of the molecule in the form of a tyrosine cluster (Tyr708, Tyr710, Tyr711, Tyr713, and Tyr715), and one site is located upstream, at Tyr569. The Tyr569 residue can autophosphorylate through an intramolecular process, whereas the tyrosine cluster cannot. The phosphorylation of Tyr569 results in an increased protein kinase activity of Wzc, which can, in turn, phosphorylate the five terminal tyrosines through an intermolecular process. It is concluded that protein Wzc autophosphorylates by using a cooperative two-step mechanism that involves both intra- and interphosphorylation. This mechanism may be of biological significance in the signal transduction mediated by Wzc.

* This work was supported by grants from the CNRS (UMR 5086), the Université de Lyon, the Région Rhône-Alpes (Emergence 97.027), the Société Ezus-Lyon 1 (Contract 482.022), and the Institut Universitaire de France.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tel.: 33-4-72-72-26-72; Fax: 33-4-72-72-26-01; E-mail: aj.cozzone@ibcp.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.