Protein kinase activity in Helicobacter pylori.
Based on the predictive analysis of the cellular protein content from the complete genome sequence of Helicobacter pylori, discrepant results were previously reported concerning the occurrence of a protein kinase in this bacterium. To solve this ambiguity, we have directly assayed cellular extracts for their capacity of phosphorylating endogenous proteins. At least eight different proteins, ranging from 24 to 200 kDa, were found to be phosphorylated to a varying extent. Individual measurement of their phosphoamino acid composition showed that they all were modified at serine residues. These data indicate that H. pylori does contain a protein-serine kinase activity.
Grangeasse
C
C
Service de Génétique Appliquée, Université Libre de Bruxelles, Nivelles, Belgium. cgrange@sga.ulb.ac.be
Pichon
B
B
Bollen
A
A
Godfroid
E
E
D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D016480:Helicobacter pylori / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000032:analysis*
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D011494:Protein Kinases