ArticleProceedings of the National Academy of Sciences of the United States of America2024
Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- From phenomenon to mechanism in the circadian clock of Synechococcus elongatus.Npj biological timing and sleep · 2026Review
- Fold-Switching Proteins.Annual review of biophysics · 2026Review
- Effects of sodium chloride on circadian period and temperature compensation of KaiC phosphorylation.Scientific reports · 2026Article
- Article
- Time-Series RNA Sequencing Reveals Temperature-Specific and Temperature-Compensated Circadian Genes inbioRxiv : the preprint server for biology · 2025Article
- SLAE: Strictly Local All-atom Environment for Protein Representation.bioRxiv : the preprint server for biology · 2025Article
- Fold-switching proteins.ArXiv · 2025Article
- Unveiling the cold reality of metamorphic proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Compensated Clock: Temperature and Nutritional Compensation Mechanisms Across Circadian Systems.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- 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
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16 authors.
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Abstract
The oscillator of the cyanobacterial circadian clock relies on the ability of the KaiB protein to switch reversibly between a stable ground-state fold (gsKaiB) and an unstable fold-switched fold (fsKaiB). Rare fold-switching events by KaiB provide a critical delay in the negative feedback loop of this posttranslational oscillator. In this study, we experimentally and computationally investigate the temperature dependence of fold switching and its mechanism. We demonstrate that the stability of gsKaiB increases with temperature compared to fsKaiB and that the Q10 value for the gsKaiB → fsKaiB transition is nearly three times smaller than that for the reverse transition in a construct optimized for NMR studies. Simulations and native-state hydrogen-deuterium exchange NMR experiments suggest that fold switching can involve both partially and completely unfolded intermediates. The simulations predict that the transition state for fold switching coincides with isomerization of conserved prolines in the most rapidly exchanging region, and we confirm experimentally that proline isomerization is a rate-limiting step for fold switching. We explore the implications of our results for temperature compensation, a hallmark of circadian clocks, through a kinetic model.
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