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