ArticleProceedings of the National Academy of Sciences of the United States of America2020
Tuning the circadian period of cyanobacteria up to 6.6 days by the single amino acid substitutions in KaiC.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 46 citations in OpenAlex.
- The Phenotypic Landscape of a Circadian Clock.bioRxiv : the preprint server for biology · 2026Article
- Intrinsic period stability of the cyanobacterial circadian oscillator across in vitro and in vivo conditions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Centriole Biogenesis Cycle: Temporal Mechanisms, Autonomy and Coupling to the Cell Cycle and Other Cellular Clocks.Advances in experimental medicine and biology · 2026Review
- Effect of pH on the cyanobacterial circadian oscillator in vitro.Communications biology · 2025Article
- Evolutionary origins of self-sustained Kai protein circadian oscillators in cyanobacteria.Nature communications · 2025Article
- Environmental and molecular noise buffering by the cyanobacterial clock in individual cells.Nature communications · 2025Article
- A Compensated Clock: Temperature and Nutritional Compensation Mechanisms Across Circadian Systems.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Programming scheduled self-assembly of circadian materials.Nature communications · 2025Article
- The cyanobacterial circadian clock.Npj biological timing and sleep · 2025Review
- Cold-induced degradation of core clock proteins implements temperature compensation in theScience advances · 2024Article
- Temperature compensation through kinetic regulation in biochemical oscillators.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- The inner workings of an ancient biological clock.Trends in biochemical sciences · 2024Review
- Article
- Emerging tools for uncovering genetic and transcriptomic heterogeneities in bacteria.Biophysical reviews · 2024Review
- KidA, a multi-PAS domain protein, tunes the period of the cyanobacterial circadian oscillator.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- 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
- Circadian rhythms in infectious diseases and symbiosis.Seminars in cell & developmental biology · 2022Review
- Regulation mechanisms of the dual ATPase in KaiC.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The circadian clock of cyanobacteria consists of only three clock proteins, KaiA, KaiB, and KaiC, which generate a circadian rhythm of KaiC phosphorylation in vitro. The adenosine triphosphatase (ATPase) activity of KaiC is the source of the 24-h period and temperature compensation. Although numerous circadian mutants of KaiC have been identified, the tuning mechanism of the 24-h period remains unclear. Here, we show that the circadian period of in vitro phosphorylation rhythm of mutants at position 402 of KaiC changed dramatically, from 15 h (0.6 d) to 158 h (6.6 d). The ATPase activities of mutants at position 402 of KaiC, without KaiA and KaiB, correlated with the frequencies (1/period), indicating that KaiC structure was the source of extra period change. Despite the wide-range tunability, temperature compensation of both the circadian period and the KaiC ATPase activity of mutants at position 402 of KaiC were nearly intact. We also found that in vivo and in vitro circadian periods and the KaiC ATPase activity of mutants at position 402 of KaiC showed a correlation with the side-chain volume of the amino acid at position 402 of KaiC. Our results indicate that residue 402 is a key position of determining the circadian period of cyanobacteria, and it is possible to dramatically alter the period of KaiC while maintaining temperature compensation.
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