ArticleScientific reports2016
A dynamic interaction process between KaiA and KaiC is critical to the cyanobacterial circadian oscillator.
Article in Scientific reports, 2016. 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.
- Programming scheduled self-assembly of circadian materials.Nature communications · 2025Article
- Two KaiABC systems control circadian oscillations in one cyanobacterium.Nature communications · 2024Article
- Article
- Perfecting the Life Clock: The Journey from PTO to TTFL.International journal of molecular sciences · 2023Review
- Intrinsically Disordered Proteins: Critical Components of the Wetware.Chemical reviews · 2022Review
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- Protein conformational dynamics and phenotypic switching.Biophysical reviews · 2021Review
- Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation.Molecules (Basel, Switzerland) · 2019Article
- The influence of KaiA mutations on its function in the KaiABC circadian clock system.Data in brief · 2018Article
- Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Expression and Purification of Cyanobacterial Circadian Clock Protein KaiC and Determination of Its Auto-phosphatase Activity.Bio-protocol · 2017Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The core circadian oscillator of cyanobacteria consists of three proteins, KaiA, KaiB, and KaiC. This circadian oscillator could be functionally reconstituted in vitro with these three proteins, and therefore has been a very important model in circadian rhythm research. KaiA can bind to KaiC and then stimulate its phosphorylation, but their interaction mechanism remains elusive. In this study, we followed the "second-site suppressor" strategy to investigate the interaction mechanism of KaiA and KaiC. Using protein sequence analyses, we showed that there exist co-varying residues in the binding interface of KaiA and KaiC. The followed mutagenesis study verified that these residues are important to the functions of KaiA and KaiC, but their roles could not be fully explained by the reported complex structures of KaiA and KaiC derived peptides. Combining our data with previous reports, we suggested a dynamic interaction mechanism in KaiA-KaiC interaction, in which both KaiA and the intrinsically disordered tail of KaiC undergo significant structural changes through conformational selection and induced fit during the binding process. At last, we presented a mathematic model to support this hypothesis and explained the importance of this interaction mechanism for the KaiABC circadian oscillator.
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