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Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a phosphotyrosine-protein phosphatase, Wzb.

C Vincent1, P Doublet, C Grangeasse

  • 1Institut de Biologie et Chimie des Protéines, Centre National de la Recherche Scientifique, Lyon, France.

Journal of Bacteriology
|May 29, 1999
PubMed
Summary
This summary is machine-generated.

Escherichia coli possesses a protein-tyrosine kinase (Wzc) and a phosphotyrosine-protein phosphatase (Wzb), revealing a novel regulatory mechanism. This reversible protein phosphorylation may influence bacterial pathogenicity.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Escherichia coli protein Wzc autophosphorylates exclusively on tyrosine.
  • Escherichia coli protein Wzb exhibits phosphotyrosine-protein phosphatase activity.
  • Wzb specifically dephosphorylates phosphotyrosine, including autophosphorylated Wzc.

Purpose of the Study:

  • To investigate the roles of Wzc and Wzb in protein phosphorylation.
  • To identify kinase and phosphatase activities in E. coli.
  • To explore the implications of tyrosine phosphorylation in bacterial pathogenicity.

Main Methods:

  • Protein overproduction and purification (affinity chromatography).
  • Autophosphorylation assays using radioactive ATP.
  • Phosphoamino acid analysis (two-dimensional).
  • Enzyme kinetics and substrate specificity assays.

Main Results:

  • Wzc demonstrates autophosphorylation activity, exclusively at tyrosine residues.
  • Wzb possesses phosphatase activity, specifically targeting phosphotyrosine.
  • Wzb effectively dephosphorylates Wzc, indicating an endogenous substrate.
  • Discovery of both a protein-tyrosine kinase and a phosphotyrosine-protein phosphatase in E. coli.

Conclusions:

  • E. coli contains a functional protein-tyrosine kinase (Wzc) and phosphotyrosine-protein phosphatase (Wzb).
  • A regulatory mechanism involving reversible tyrosine phosphorylation is suggested, with Wzb acting on Wzc.
  • Tyrosine phosphorylation may play a role in bacterial virulence, potentially linked to exopolysaccharide synthesis.