ArticleProceedings of the National Academy of Sciences of the United States of America2014
Exchange of ADP with ATP in the CII ATPase domain promotes autophosphorylation of cyanobacterial clock protein KaiC.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 45 citations in OpenAlex.
- An underlying bistability sets amplitude and explains temperature compensation in the cyanobacterial circadian clock.bioRxiv : the preprint server for biology · 2026Article
- Effect of pH on the cyanobacterial circadian oscillator in vitro.Communications biology · 2025Article
- The cyanobacterial circadian clock.Npj biological timing and sleep · 2025Review
- A topological mechanism for robust and efficient global oscillations in biological networks.Nature communications · 2024Article
- The inner workings of an ancient biological clock.Trends in biochemical sciences · 2024Review
- Article
- From primordial clocks to circadian oscillators.Nature · 2023Article
- Robust replication initiation from coupled homeostatic mechanisms.Nature communications · 2022Article
- Coupling of distant ATPase domains in the circadian clock protein KaiC.Nature structural & molecular biology · 2022Article
- Regulation mechanisms of the dual ATPase in KaiC.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Dimer dissociation is a key energetic event in the fold-switch pathway of KaiB.Biophysical journal · 2022Article
- Monitoring Protein-Protein Interactions in the Cyanobacterial Circadian Clock in Real Time via Electron Paramagnetic Resonance Spectroscopy.Biochemistry · 2020Article
- 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
- 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
- Revealing circadian mechanisms of integration and resilience by visualizing clock proteins working in real time.Nature communications · 2018Article
- Structure, function, and mechanism of the core circadian clock in cyanobacteria.The Journal of biological chemistry · 2018Review
- Minimal tool set for a prokaryotic circadian clock.BMC evolutionary biology · 2017Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyanobacterial circadian oscillator can be reconstituted in vitro. In the presence of KaiA and KaiB, the phosphorylation state of KaiC oscillates with a periodicity of ∼24 h. KaiC is a hexameric P-loop ATPase with autophosphorylation and autodephosphorylation activities. Recently, we found that dephosphorylation of KaiC occurs via reversal of the phosphorylation reaction: a phosphate group attached to Ser431/Thr432 is transferred to KaiC-bound ADP to generate ATP, which is subsequently hydrolyzed. This unusual reaction mechanism suggests that the KaiC phosphorylation rhythm is sustained by periodic shifts in the equilibrium of the reversible autophosphorylation reaction, the molecular basis of which has never been elucidated. Because KaiC-bound ATP and ADP serve as substrates for the forward and reverse reactions, respectively, we investigated the regulation of the nucleotide-bound state of KaiC. In the absence of KaiA, the condition in which the reverse reaction proceeds, KaiC favored the ADP-bound state. KaiA increased the ratio of ATP to total KaiC-bound nucleotides by facilitating the release of bound ADP and the incorporation of exogenous ATP, allowing the forward reaction to proceed. When both KaiA and KaiB were present, the ratio of ATP to total bound nucleotides exhibited a circadian rhythm, whose phase was advanced by several hours relative to that of the phosphorylation rhythm. Based on these findings, we propose that the direction of the reversible autophosphorylation reaction is regulated by KaiA and KaiB at the level of substrate availability and that this regulation sustains the oscillation of the phosphorylation state of KaiC.
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