2015 Fiscal Year Final Research Report
Signal transduction through tyrosine phosphorylation in Myxobacteria
| Project/Area Number |
25440087
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Kagawa University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
Takegawa Kaoru 九州大学, 農学研究科大学院, 教授 (50197282)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Keywords | 粘液細菌 / 真核生物様プロテインキナーゼ / 細菌型チロシンキナーゼ / チロシンホスファターゼ |
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| Outline of Final Research Achievements |
Seven out of 14 recombinant Myxococcus xanthus eukaryotic-like protein kinases containing atypical motifs in the catalytic loop showed protein kinase activity and four autophosphorylated EPKs were detected using anti-phosphotyrosine antibody by western blotting. However, these kinases did not show Tyr kinase activity against myelin basic protein. In two kinases, autophosphorylation on Tyr residues was required for high-level kinase activity. Also, we suggested that two bacterial protein-tyrosine (BY) kinases, BtkA and BtkB, are activated by the intracellular juxtamembrane regions of the second transmembrane helices in receptors. A btkB mutant constructed by replacing all C-terminal Tyr residues with Phe did not significantly affect kinase activity, suggesting that M. xanthus BtkB kinase activity is not dependent on autophosphorylation in the C-terminal Tyr cluster. Finally, we indicated that PrpA, which is an ApaH-like phosphatase, function as a tyrosine protein phosphatase.wo
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| Free Research Field |
微生物学
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