ArticleScientific reports2018
Conformational rearrangements of the C1 ring in KaiC measure the timing of assembly with KaiB.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Reconstitution of circadian clock in synthetic cells reveals principles of timekeeping.Nature communications · 2025Article
- The priming phosphorylation of KaiC is activated by the release of its autokinase autoinhibition.PNAS nexus · 2025Article
- The cyanobacterial circadian clock.Npj biological timing and sleep · 2025Review
- Review
- Role of the reaction-structure coupling in temperature compensation of the KaiABC circadian rhythm.PLoS computational biology · 2022Article
- Coupling of distant ATPase domains in the circadian clock protein KaiC.Nature structural & molecular biology · 2022Article
- Highly sensitive tryptophan fluorescence probe for detecting rhythmic conformational changes of KaiC in the cyanobacterial circadian clock system.The Biochemical journal · 2022Article
- Regulation mechanisms of the dual ATPase in KaiC.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multimeric structure enables the acceleration of KaiB-KaiC complex formation induced by ADP/ATP exchange inhibition.PLoS computational biology · 2022Article
- Slow and temperature-compensated autonomous disassembly of KaiB-KaiC complex.Biophysics and physicobiology · 2022Article
- Mechanism of autonomous synchronization of the circadian KaiABC rhythm.Scientific reports · 2021Article
- Bayesian modeling reveals metabolite-dependent ultrasensitivity in the cyanobacterial circadian clock.Molecular systems biology · 2020Article
- Orchestration of Circadian Timing by Macromolecular Protein Assemblies.Journal of molecular biology · 2020Review
- Pressure accelerates the circadian clock of cyanobacteria.Scientific reports · 2019Article
- ATP hydrolysis by KaiC promotes its KaiA binding in the cyanobacterial circadian clock system.Life science alliance · 2019Article
- Review
- Molecular dynamics simulations of nucleotide release from the circadian clock protein KaiC reveal atomic-resolution functional insights.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KaiC, the core oscillator of the cyanobacterial circadian clock, is composed of an N-terminal C1 domain and a C-terminal C2 domain, and assembles into a double-ring hexamer upon ATP binding. Cyclic phosphorylation and dephosphorylation at Ser431 and Thr432 in the C2 domain proceed with a period of approximately 24 h in the presence of other clock proteins, KaiA and KaiB, but recent studies have revealed a crucial role for the C1 ring in determining the cycle period. In this study, we mapped dynamic structural changes of the C1 ring in solution using a combination of site-directed tryptophan mutagenesis and fluorescence spectroscopy. We found that the C1 ring undergoes a structural transition, coupled with ATPase activity and the phosphorylation state, while maintaining its hexameric ring structure. This transition triggered by ATP hydrolysis in the C1 ring in specific phosphorylation states is a necessary event for recruitment of KaiB, limiting the overall rate of slow complex formation. Our results provide structural and kinetic insights into the C1-ring rearrangements governing the slow dynamics of the cyanobacterial circadian clock.
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