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Article

ATPase activity of KaiC determines the basic timing for circadian clock of cyanobacteria.

Proceedings of the National Academy of Sciences of the United States of America - 9 Oct 2007

Terauchi Kazuki, Kitayama Yohko, Nishiwaki Taeko, Miwa Kumiko, Murayama Yoriko, Oyama Tokitaka, Kondo Takao

Abstract excerpt

Self-sustainable oscillation of KaiC phosphorylation has been reconstituted in vitro, demonstrating that this cycle is the basic time generator of the circadian clock of cyanobacteria. Here we show that the ATPase activity of KaiC satisfies the characteristics of the circadian oscillation, the period length, and the temperature compensation. KaiC possesses extremely weak but stable ATPase activity (15 molecules...

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Identifiers

PMID: 17901204
DOI: 10.1073/pnas.0706292104
PMCID: PMC2042214

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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ATPase activity of KaiC determines the basic timing for circadian clock of cyanobacteria.PMID 17901204Read ↗

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Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro.Semantic proximity Read ↗

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KaiA-stimulated KaiC phosphorylation in circadian timing loops in cyanobacteria.Semantic proximity Read ↗

Dephosphorylation of the core clock protein KaiC in the cyanobacterial KaiABC circadian oscillator proceeds via an ATP synthase mechanism.Semantic proximity Read ↗

Circadian clocks go in vitro: purely post-translational oscillators in cyanobacteria.Semantic proximity Read ↗

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