ArticleBiochemistry2013
Loop-loop interactions regulate KaiA-stimulated KaiC phosphorylation in the cyanobacterial KaiABC circadian clock.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- The free-running property of circadian clocks is needed to tolerate changing photoperiods.Current biology : CB · 2026Article
- KaiC family ATPases in the nonheterocystous nitrogen-fixing cyanobacterium Leptolyngbya boryana.Scientific reports · 2024Article
- Photomorphogenesis of Myxococcus macrosporus: new insights for light-regulation of cell development.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024Article
- Determining subunit-subunit interaction from statistics of cryo-EM images: observation of nearest-neighbor coupling in a circadian clock protein complex.Nature communications · 2023Article
- From primordial clocks to circadian oscillators.Nature · 2023Article
- Synchronization of the circadian clock to the environment tracked in real time.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.Science advances · 2022Article
- Dimer dissociation is a key energetic event in the fold-switch pathway of KaiB.Biophysical journal · 2022Article
- Shift in Conformational Equilibrium Underlies the Oscillatory Phosphoryl Transfer Reaction in the Circadian Clock.Life (Basel, Switzerland) · 2021Article
- ATP hydrolysis by KaiC promotes its KaiA binding in the cyanobacterial circadian clock system.Life science alliance · 2019Article
- Molecular dynamics simulations of nucleotide release from the circadian clock protein KaiC reveal atomic-resolution functional insights.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structure, function, and mechanism of the core circadian clock in cyanobacteria.The Journal of biological chemistry · 2018Review
- Minimal tool set for a prokaryotic circadian clock.BMC evolutionary biology · 2017Article
- Architecture and mechanism of the central gear in an ancient molecular timer.Journal of the Royal Society, Interface · 2017Review
- A thermodynamically consistent model of the post-translational Kai circadian clock.PLoS computational biology · 2017Article
- Mixtures of opposing phosphorylations within hexamers precisely time feedback in the cyanobacterial circadian clock.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Intricate protein-protein interactions in the cyanobacterial circadian clock.The Journal of biological chemistry · 2014Review
- An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.Acta crystallographica. Section D, Biological crystallography · 2014Article
- A circadian clock nanomachine that runs without transcription or translation.Current opinion in neurobiology · 2013Review
- CryoEM and molecular dynamics of the circadian KaiB-KaiC complex indicates that KaiB monomers interact with KaiC and block ATP binding clefts.Journal of molecular biology · 2013Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The Synechococcus elongatus KaiA, KaiB, and KaiC proteins in the presence of ATP generate a post-translational oscillator that runs in a temperature-compensated manner with a period of 24 h. KaiA dimer stimulates phosphorylation of KaiC hexamer at two sites per subunit, T432 and S431, and KaiB dimers antagonize KaiA action and induce KaiC subunit exchange. Neither the mechanism of KaiA-stimulated KaiC phosphorylation nor that of KaiB-mediated KaiC dephosphorylation is understood in detail at present. We demonstrate here that the A422V KaiC mutant sheds light on the former mechanism. It was previously reported that A422V is less sensitive to dark pulse-induced phase resetting and has a reduced amplitude of the KaiC phosphorylation rhythm in vivo. A422 maps to a loop (422-loop) that continues toward the phosphorylation sites. By pulling on the C-terminal peptide of KaiC (A-loop), KaiA removes restraints from the adjacent 422-loop whose increased flexibility indirectly promotes kinase activity. We found in the crystal structure that A422V KaiC lacks phosphorylation at S431 and exhibits a subtle, local conformational change relative to wild-type KaiC. Molecular dynamics simulations indicate higher mobility of the 422-loop in the absence of the A-loop and mobility differences in other areas associated with phosphorylation activity between wild-type and mutant KaiCs. The A-loop-422-loop relay that informs KaiC phosphorylation sites of KaiA dimer binding propagates to loops from neighboring KaiC subunits, thus providing support for a concerted allosteric mechanism of phosphorylation.
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