期刊
EMBO JOURNAL
卷 30, 期 1, 页码 68-78出版社
WILEY
DOI: 10.1038/emboj.2010.298
关键词
ATPase; circadian clock; phosphorylation; small-angle X-ray scattering; temperature compensation
资金
- Japan Society for the Promotion of Science
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT) of Japan [22687010, 19042011, 20570035, 21023011]
- Japan Science and Technology Agency
- Grants-in-Aid for Scientific Research [20570035, 19042011, 21023011, 22687010] Funding Source: KAKEN
The circadian clock in cyanobacteria persists even without the transcription/translation feedbacks proposed for eukaryotic systems. The period of the cyanobacterial clock is tuned to the circadian range by the ATPase activity of a clock protein known as KaiC. Here, we provide structural evidence on how KaiC ticks away 24 h while coupling the ATPase activity in its N-terminal ring to the phosphorylation state in its C-terminal ring. During the phosphorylation cycle, the C-terminal domains of KaiC are repositioned in a stepwise manner to affect global expansion and contraction motions of the C-terminal ring. Arg393 of KaiC has a critical function in expanding the C-terminal ring and its replacement with Cys affects the temperature compensation of the period-a fundamental property of circadian clocks. The conformational ticking of KaiC observed here in solution serves as a timing cue for assembly/disassembly of other clock proteins (KaiA and KaiB), and is interlocked with its auto-inhibitory ATPase underlying circadian periodicity of cyanobacteria. The EMBO Journal (2011) 30, 68-78. doi:10.1038/emboj.2010.298; Published online 26 November 2010
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