In vitro regulation of circadian phosphorylation rhythm of cyanobacterial clock protein KaiC by KaiA and KaiB

Masato Nakajima, Hiroshi Ito, Takao Kondo

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

Biochemical circadian oscillation of KaiC phosphorylation, by mixing three Kai proteins and ATP, has been proven to be the central oscillator of the cyanobacterial circadian clock. In vivo, the intracellular levels of KaiB and KaiC oscillate in a circadian fashion. By scrutinizing KaiC phosphorylation rhythm in a wide range of Kai protein concentrations, KaiA and KaiB were found to be "parameter-tuning" and "state-switching" regulators of KaiC phosphorylation rhythm, respectively. Our results also suggest a possible entrainment mechanism of the cellular circadian clock with the circadian variation of intracellular levels of Kai proteins.

Original languageEnglish
Pages (from-to)898-902
Number of pages5
JournalFEBS Letters
Volume584
Issue number5
DOIs
Publication statusPublished - Mar 5 2010
Externally publishedYes

Fingerprint

Phosphorylation
Circadian Rhythm
Clocks
Circadian Clocks
Proteins
Tuning
Adenosine Triphosphate
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

In vitro regulation of circadian phosphorylation rhythm of cyanobacterial clock protein KaiC by KaiA and KaiB. / Nakajima, Masato; Ito, Hiroshi; Kondo, Takao.

In: FEBS Letters, Vol. 584, No. 5, 05.03.2010, p. 898-902.

Research output: Contribution to journalArticle

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