| Project/Area Number |
04833008
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
分子細胞生物学
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| Research Institution | Kanazawa University |
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Principal Investigator |
YASUDA Hideyo Kanazawa University, Faculty of Pharmaceutical Sciences, Associate Professor, 薬学部, 助教授 (40111554)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1993: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1992: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | cdk / cyclin / cdc2 kinase / phosphorylation / cell cycle / cdk / cdk2 / AP1 / 転写制御 |
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| Research Abstract |
The activity of cdc2 kinase is regulated by the phosphorylation and dephosphorylation of its own molecule. The phosphorylation of Thr-14 and/or Tyr-15 inhibits the kinase activity, whereas the phosphorylation of Thr-161 is necessary for the activity of this kinase. We tried to find out the kinase which phosphorylated the cdc2 kinase and inhibited the activity. Human weel kinase had such kind of activity. The kinase could phosphorylate Try-15 of the cdc2 molecule but not do Thr-14. The kinase which could phosphorylate Thr-14 now to be elucidated. The enzyme which phosphorylates this Trh-161 is named CAK(cyclin dependent kinase activating kinase). Recent work revealed Xenopus laevis p40MO15 kinase could phosphorylate this residue and activate the kinase. The DNA sequence of this kinase is homologus to that of R-2 protein which was isolated from rice cells as one of the cdks. We tried to clarify whether this R-2 protein has kinase activity to activate the cdc2 kinase. We found the R-2 kinase, which was produced in E.coli, could activate the HeLa cdc2 kinase in the presence of cyclin B.Also we isolated the mouse homologue of p40MO15. These kinases had NXTALRE sequence in stead of PSTAIRE of cdc2 kinase.
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