ArticlePLoS computational biology2022
Role of the reaction-structure coupling in temperature compensation of the KaiABC circadian rhythm.
Article in PLoS computational biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 8 citations in OpenAlex.
- Waveform distortion for temperature compensation and synchronization in circadian rhythms: An approach based on the renormalization group method.PLoS computational biology · 2025Article
- When lowering temperature, the in vivo circadian clock in cyanobacteria follows and surpasses the in vitro protein clock trough the Hopf bifurcation.Scientific reports · 2025Article
- Leveraging Sequence Purification for Accurate Prediction of Multiple Conformational States with AlphaFold2.Research square · 2025Article
- A Compensated Clock: Temperature and Nutritional Compensation Mechanisms Across Circadian Systems.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Computation Implemented by the Interaction of Chemical Reaction, Clustering, and De-Clustering of Molecules.Biomimetics (Basel, Switzerland) · 2024Article
- Temperature compensation through kinetic regulation in biochemical oscillators.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structure-function relationship of KaiC around dawn.Biophysics and physicobiology · 2024Article
- Artificial temperature-compensated biological clock using temperature-sensitive Belousov-Zhabotinsky gels.Scientific reports · 2022Article
- Beyond multi-disciplinary and cross-scale analyses of the cyanobacterial circadian clock system.Biophysics and physicobiology · 2021Article
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
When the mixture solution of cyanobacterial proteins, KaiA, KaiB, and KaiC, is incubated with ATP in vitro, the phosphorylation level of KaiC shows stable oscillations with the temperature-compensated circadian period. Elucidating this temperature compensation is essential for understanding the KaiABC circadian clock, but its mechanism has remained a mystery. We analyzed the KaiABC temperature compensation by developing a theoretical model describing the feedback relations among reactions and structural transitions in the KaiC molecule. The model showed that the reduced structural cooperativity should weaken the negative feedback coupling among reactions and structural transitions, which enlarges the oscillation amplitude and period, explaining the observed significant period extension upon single amino-acid residue substitution. We propose that an increase in thermal fluctuations similarly attenuates the reaction-structure feedback, explaining the temperature compensation in the KaiABC clock. The model explained the experimentally observed responses of the oscillation phase to the temperature shift or the ADP-concentration change and suggested that the ATPase reactions in the CI domain of KaiC affect the period depending on how the reaction rates are modulated. The KaiABC clock provides a unique opportunity to analyze how the reaction-structure coupling regulates the system-level synchronized oscillations of molecules.
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