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Papers In Press, published online ahead of print December 20, 2001
Molecular Biology, C.N.R.S. - University of Lyon, LYON 69007
Corresponding Author: aj.cozzone{at}ibcp.fr
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 trans-membrane a-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 6 different sites of phosphorylation. Among these, 5 are located at the C-end of the molecule in the form of a tyrosine cluster (Y708, Y710, Y711, Y713, and Y715), and one site is located upstream, at Y569. The Y569 residue can autophosphorylate through an intramolecular process, whereas the tyrosine cluster cannot. The phosphorylation of Y569 results in an increased protein-kinase activity of Wzc which can, in turn, phosphorylate the 5 terminal tyrosines through an intermolecular process. It is concluded that protein Wzc autophosphorylates by using a cooperative two-step mechanism which involves both intraphosphorylation and interphosphorylation. This mechanism may be of biological significance in the signal transduction mediated by Wzc.
J. Biol. Chem, 10.1074/jbc.M110880200
Submitted on November 13, 2001
Revised on December 18, 2001
Accepted on December 20, 2001
Tyrosine phosphorylation of protein kinase Wzc from E. coli K12 occurs through a two-step process
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