Protein kinase activity in Helicobacter pylori

Abstract 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...

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Bibliographic Details
Published in:FEMS microbiology letters 1999-07, Vol.176 (2), p.327-332
Main Authors: Grangeasse, Christophe, Pichon, Bruno, Bollen, Alex, Godfroid, Edmond
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Bacterial protein phosphorylation
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Genomes
Helicobacter pylori
Helicobacter pylori - enzymology
Kinases
Metabolism. Enzymes
Microbiology
Nucleotide sequence
Phosphorylation
Protein kinase
Protein Kinases - analysis
Protein-serine kinase
Proteins
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Summary:Abstract 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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1999.tb13679.x