ArticleJournal of molecular biology2014
Cooperative KaiA-KaiB-KaiC interactions affect KaiB/SasA competition in the circadian clock of cyanobacteria.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- From phenomenon to mechanism in the circadian clock of Synechococcus elongatus.Npj biological timing and sleep · 2026Review
- Cyanobacterial Circadian Clock: Molecular Mechanisms and Physiological Outputs.Plants (Basel, Switzerland) · 2026Review
- The Phenotypic Landscape of a Circadian Clock.bioRxiv : the preprint server for biology · 2026Article
- The free-running property of circadian clocks is needed to tolerate changing photoperiods.Current biology : CB · 2026Article
- Reconstitution of circadian clock in synthetic cells reveals principles of timekeeping.Nature communications · 2025Article
- The cyanobacterial circadian clock.Npj biological timing and sleep · 2025Review
- Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Two KaiABC systems control circadian oscillations in one cyanobacterium.Nature communications · 2024Article
- 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
- Roles for theJournal of biological rhythms · 2023Article
- Determining subunit-subunit interaction from statistics of cryo-EM images: observation of nearest-neighbor coupling in a circadian clock protein complex.Nature communications · 2023Article
- Synchronization of the circadian clock to the environment tracked in real time.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Coupling of distant ATPase domains in the circadian clock protein KaiC.Nature structural & molecular biology · 2022Article
- Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.Science advances · 2022Article
- Multimeric structure enables the acceleration of KaiB-KaiC complex formation induced by ADP/ATP exchange inhibition.PLoS computational biology · 2022Article
- Evolution of the repression mechanisms in circadian clocks.Genome biology · 2022Article
- Shift in Conformational Equilibrium Underlies the Oscillatory Phosphoryl Transfer Reaction in the Circadian Clock.Life (Basel, Switzerland) · 2021Article
- Reconstitution of an intact clock reveals mechanisms of circadian timekeeping.Science (New York, N.Y.) · 2021Article
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7 authors.
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Abstract
The circadian oscillator of cyanobacteria is composed of only three proteins, KaiA, KaiB, and KaiC. Together, they generate an autonomous ~24-h biochemical rhythm of phosphorylation of KaiC. KaiA stimulates KaiC phosphorylation by binding to the so-called A-loops of KaiC, whereas KaiB sequesters KaiA in a KaiABC complex far away from the A-loops, thereby inducing KaiC dephosphorylation. The switch from KaiC phosphorylation to dephosphorylation is initiated by the formation of the KaiB-KaiC complex, which occurs upon phosphorylation of the S431 residues of KaiC. We show here that formation of the KaiB-KaiC complex is promoted by KaiA, suggesting cooperativity in the initiation of the dephosphorylation complex. In the KaiA-KaiB interaction, one monomeric subunit of KaiB likely binds to one face of a KaiA dimer, leaving the other face unoccupied. We also show that the A-loops of KaiC exist in a dynamic equilibrium between KaiA-accessible exposed and KaiA-inaccessible buried positions. Phosphorylation at the S431 residues of KaiC shift the A-loops toward the buried position, thereby weakening the KaiA-KaiC interaction, which is expected to be an additional mechanism promoting formation of the KaiABC complex. We also show that KaiB and the clock-output protein SasA compete for overlapping binding sites, which include the B-loops on the CI ring of KaiC. KaiA strongly shifts the competition in KaiB's favor. Thus, in addition to stimulating KaiC phosphorylation, it is likely that KaiA plays roles in switching KaiC from phosphorylation to dephosphorylation, as well as regulating clock output.
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