PhpA, a tyrosine phosphatase of Myxococcus xanthus, is involved in the production of exopolysaccharide

Yumi Mori, Miri Maeda, Kaoru Takegawa, Yoshio Kimura

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Protein-tyrosine phosphorylation plays a significant role in multiple cellular functions in bacteria. Bacterial tyrosine phosphatases catalyse the dephosphorylation of tyrosyl-phosphorylated proteins. Myxococcus xanthus PhpA shares homology with DNA polymerase and histidinol phosphatase family members. Recombinant His-tagged PhpA requires Mn2+ or Co2+ for phosphatase activity, and shows strict specificity for phosphorylated tyrosine residues. The km values of PhpA for p-nitrophenyl phosphate (pNPP) and phosphotyrosine peptide, RRLIEDAEpYAARG, were 803 and 139 μM, respectively. The phosphatase activity of PhpA was inhibited by sodium orthovanadate with a ki of 33 μM. phpA gene expression was observed under both vegetative and developmental conditions, but peaked during late fruiting body formation. A phpA mutant exhibited an elevated level of tyrosine phosphorylation of a 79 kDa protein and cytoplasmic tyrosine kinase, BtkA. In M. xanthus, exopolysaccharide (EPS) is essential for cell-cell adhesion and fruiting body formation. phpA mutant cells exhibited enhanced capacity for cell- cell agglutination in agglutination buffer. Under starvation conditions, phpA mutation caused early aggregation and sporulation. The EPS production assay showed that the phpA mutant produced an increased amount of EPS in comparison with the wild-type. These results indicate that PhpA may negatively regulate the production of EPS in M. xanthus.

Original languageEnglish
Pages (from-to)2546-2555
Number of pages10
JournalMicrobiology (United Kingdom)
Volume158
Issue number10
DOIs
Publication statusPublished - Oct 1 2012

All Science Journal Classification (ASJC) codes

  • Microbiology

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