Study on Function of Eukaryotic Protein Kinase and Phosphatase in Firmicutes

2015 Fiscal Year Final Research Report

• Project/Area Number: 25460535
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Bacteriology (including mycology)
• Research Institution: Kagawa University
• Principal Investigator: NARIYA HIROFUMI 香川大学, 医学部, 助教(学内講師) (30452668)
• Co-Investigator(Kenkyū-buntansha): TAMAI EIJI 松山大学, 薬学部, 准教授 (40333512)
• Project Period (FY): 2013-04-01 – 2016-03-31
• 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.

Free Research Field

細菌学、生化学、分子微生物学、応用微生物学