Literature DB >> 10427715

Protein kinase activity in Helicobacter pylori.

C Grangeasse1, B Pichon, A Bollen, E Godfroid.   

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.

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Year:  1999        PMID: 10427715     DOI: 10.1111/j.1574-6968.1999.tb13679.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  1 in total

Review 1.  Bacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicity.

Authors:  Ruiguang Ge; Weiran Shan
Journal:  Genomics Proteomics Bioinformatics       Date:  2011-10       Impact factor: 7.691

  1 in total

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