| Project/Area Number |
25840058
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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 |
Biophysics
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| Research Institution | Institute for Molecular Science |
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Principal Investigator |
MUKAIYAMA Atsushi 分子科学研究所, 協奏分子システム研究センター, 助教 (80647446)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 生物時計 / タンパク質 / 構造変化 / 時計タンパク質 / 概日リズム |
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| Outline of Final Research Achievements |
Cyanobacterial circadian clock is composed of the three proteins, KaiA, KaiB, and KaiC. In this study, we examined the structural transition of KaiC during circadian oscillation. KaiC is a hexameric protein, consisting of the two rings. Recent studies have pointed out that ATPase of N-terminal ring of KaiC functions as a circadian pacemaker. We constructed KaiC mutant in which tryptophan (Trp) was introduced at the N-terimal ring and conducted time-resolved fluorescence measurements. We found that the fluorescence intensity from an inserted Trp exhibited the rhythmic change in the presence of KaiA and KaiB. This is a clear sign of the structural transition of the N-terminal ring in solution. The oscillatory amplitude in the fluorescence intensity was subtle, which indicates that small-scale structural transition of the N-terminal ring of KaiC.
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