ArticleProceedings of the National Academy of Sciences of the United States of America2022
Regulation mechanisms of the dual ATPase in KaiC.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Effect of pH on the cyanobacterial circadian oscillator in vitro.Communications biology · 2025Article
- The priming phosphorylation of KaiC is activated by the release of its autokinase autoinhibition.PNAS nexus · 2025Article
- KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana.Scientific reports · 2024Article
- Computation Implemented by the Interaction of Chemical Reaction, Clustering, and De-Clustering of Molecules.Biomimetics (Basel, Switzerland) · 2024Article
- The inner workings of an ancient biological clock.Trends in biochemical sciences · 2024Review
- Structure-function relationship of KaiC around dawn.Biophysics and physicobiology · 2024Article
- Slow and temperature-compensated autonomous disassembly of KaiB-KaiC complex.Biophysics and physicobiology · 2022Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KaiC is a dual adenosine triphosphatase (ATPase), with one active site in its N-terminal domain and another in its C-terminal domain, that drives the circadian clock system of cyanobacteria through sophisticated coordination of the two sites. To elucidate the coordination mechanism, we studied the contribution of the dual-ATPase activities in the ring-shaped KaiC hexamer and these structural bases for activation and inactivation. At the N-terminal active site, a lytic water molecule is sequestered between the N-terminal domains, and its reactivity to adenosine triphosphate (ATP) is controlled by the quaternary structure of the N-terminal ring. The C-terminal ATPase activity is regulated mostly by water-incorporating voids between the C-terminal domains, and the size of these voids is sensitive to phosphoryl modification of S431. The up-regulatory effect on the N-terminal ATPase activity inversely correlates with the affinity of KaiC for KaiB, a clock protein constitutes the circadian oscillator together with KaiC and KaiA, and the complete dissociation of KaiB from KaiC requires KaiA-assisted activation of the dual ATPase. Delicate interactions between the N-terminal and C-terminal rings make it possible for the components of the dual ATPase to work together, thereby driving the assembly and disassembly cycle of KaiA and KaiB.
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