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J. Biol. Chem., Vol. 278, Issue 41, 39323-39329, October 10, 2003

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Autophosphorylation of the Escherichia coli Protein Kinase Wzc Regulates Tyrosine Phosphorylation of Ugd, a UDP-glucose Dehydrogenase^*

Christophe Grangeasse  , Brice Obadia , Ivan Mijakovic ¶, Josef Deutscher ¶, Alain J. Cozzone  and Patricia Doublet 

From the Institut de Biologie et Chimie des Protéines, CNRS, Université de Lyon, 69367 Lyon Cedex 07, France and ^¶Microbiologie et Génétique Moléculaire, CNRS, Institut National de la Recherche Agronomique, Institut National Agronomique Paris-Grinon, 78850 Thiverval-Grignon, France

Autophosphorylation of protein-tyrosine kinases (PTKs) involved in exopolysaccharide and capsular polysaccharide biosynthesis and transport has been observed in a number of Gram-negative and Gram-positive bacteria. However, besides their own phosphorylation, little is known about other substrates targeted by these protein-modifying enzymes. Here, we present evidence that the protein-tyrosine kinase Wzc of Escherichia coli is able to phosphorylate an endogenous enzyme, UDP-glucose dehydrogenase (Ugd), which participates in the synthesis of the exopolysaccharide colanic acid. The process of phosphorylation of Ugd by Wzc was shown to be stimulated by previous autophosphorylation of Wzc on tyrosine 569. The phosphorylation of Ugd was demonstrated to actually occur on tyrosine and result in a significant increase of its dehydrogenase activity. In addition, the phosphotyrosine-protein phosphatase Wzb, which is known to effectively dephosphorylate Wzc, exhibited only a low effect, if any, on the dephosphorylation of Ugd. These data were related to the recent observation that two other UDP-glucose dehydrogenases have been also shown to be phosphorylated by a PTK in the Gram-positive bacterium Bacillus subtilis. Comparative analysis of the activities of PTKs from Gram-negative and Gram-positive bacteria showed that they are regulated by different mechanisms that involve, respectively, either the autophosphorylation of kinases or their interaction with a membrane protein activator.

Received for publication, May 15, 2003 , and in revised form, June 20, 2003.

^* This work was supported by Ministère de la Recherche Grant FNS 2000 (Microbiologie), Région Rhône-Alpes Grant Emergence 97.027, Société Ezus-Lyon 1 Grant 482.022, and a grant from the Institut Universitaire de France. 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: Institut de Biologie et Chimie des Protéines, 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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