The elucidation of ATPase-mediated intramolecular feedback in KaiC
| Project/Area Number |
23770039
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Plant molecular biology/Plant physiology
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| Research Institution | Yokohama City University |
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Principal Investigator |
TAKAI Naoki 横浜市立大学, 生命ナノシステム科学研究科, 助教 (80580018)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | KaiC / ATPase / 生物時計 / シアノバクテリア / 概日時計 |
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| Research Abstract |
The circadian clock comprises three clock proteins named KaiA, KaiB, and KaiC. The ATPase activity of KaiC defines the period of circadian rhythms in vivo and vitro and has an essential circadian characteristic of temperature compensation. In this study, we show how the ATPase activity of KaiC keeps the period of circadian rhythms constant across broad range temperature functions. When an ATPase reaction of KaiC are initiated by a temperature jump from on-ice to 45 °C, the ATPase activity is elevated instantaneously, and soon repressed by an intramolecular feedback in itself, but nevertheless the ATPase activity in KaiC mutant that lose the characteristic of temperature compensation of the period do not show this attenuation as KaiC-WT showed. We presumed that KaiC has an intramolecular feedback mechanism using ATPase activity of C2 domain in itself, which keeps the period of circadian rhythms constant across broad range temperature.
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Report
(3 results)
Research Products
(12 results)
