2015 Fiscal Year Final Research Report
Study on Function of Eukaryotic Protein Kinase and Phosphatase in Firmicutes
Project/Area Number |
25460535
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Bacteriology (including mycology)
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Research Institution | Kagawa University |
Principal Investigator |
NARIYA HIROFUMI 香川大学, 医学部, 助教(学内講師) (30452668)
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Co-Investigator(Kenkyū-buntansha) |
TAMAI EIJI 松山大学, 薬学部, 准教授 (40333512)
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Keywords | ガス壊疽菌 / シグナル伝達 / リン酸化 / プロテインキナーゼ / プロテインホスファターゼ / Clostridium perfringens / 形態形成 / 多様性 |
Outline of Final Research Achievements |
Protein Ser/Thr Kinase (K)-Phosphatase (P) plays essential roles in regulation of cellular functions in both prokaryotes and eukaryotes. Although PP2C family P- PknB family receptor K system is conserved in Firmicutes bacteria, functional diversity of the system is implicated by its substrate (S) diversity. Our studies on the K-P system in C. perfringens revealed that S is a novel signaling factor distributing only in Clostridia and containg protein-protein interaction domains. S is phosphorylated at Thr-92 and the phosphorylated-form S is increased by according to cell-growth progression. Cell-length is corelated with the phosphorylation level of S upon the K-P system. Furthermore, S is located at septa and poles in the cells, probably associating with two essential enzymes in the cell wall synthesis pathways.
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Free Research Field |
細菌学、生化学、分子微生物学、応用微生物学
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