ArticleScientific reports2016
Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Toward Nanodisc Tailoring for SANS Study of Membrane Proteins.Bioengineering (Basel, Switzerland) · 2026Article
- Size-exclusion chromatography-small-angle neutron scattering system optimized for an instrument with medium neutron flux.Journal of applied crystallography · 2025Article
- Overall structure of fully assembled cyanobacterial KaiABC circadian clock complex by an integrated experimental-computational approach.Communications biology · 2022Article
- Elucidation of the mechanism of subunit exchange in αB crystallin oligomers.Scientific reports · 2021Article
- Deuteration Aiming for Neutron Scattering.Biophysics and physicobiology · 2021Article
- A novel experimental approach for nanostructure analysis: simultaneous small-angle X-ray and neutron scattering.Journal of applied crystallography · 2020Article
- Damped circadian oscillation in the absence of KaiA in Synechococcus.Nature communications · 2020Article
- Supramolecular tholos-like architecture constituted by archaeal proteins without functional annotation.Scientific reports · 2020Article
- Cooperative Binding of KaiB to the KaiC Hexamer Ensures Accurate Circadian Clock Oscillation in Cyanobacteria.International journal of molecular sciences · 2019Article
- ATP hydrolysis by KaiC promotes its KaiA binding in the cyanobacterial circadian clock system.Life science alliance · 2019Article
- Structure, function, and mechanism of the core circadian clock in cyanobacteria.The Journal of biological chemistry · 2018Review
- Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering.Biochemistry and biophysics reports · 2017Article
- Structural basis of the day-night transition in a bacterial circadian clock.Science (New York, N.Y.) · 2017Article
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Authors and funding
15 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular machinery of the cyanobacterial circadian clock consists of three proteins: KaiA, KaiB, and KaiC. Through interactions among the three Kai proteins, the phosphorylation states of KaiC generate circadian oscillations in vitro in the presence of ATP. Here, we characterized the complex formation between KaiB and KaiC using a phospho-mimicking mutant of KaiC, which had an aspartate substitution at the Ser431 phosphorylation site and exhibited optimal binding to KaiB. Mass-spectrometric titration data showed that the proteins formed a complex exclusively in a 6:6 stoichiometry, indicating that KaiB bound to the KaiC hexamer with strong positive cooperativity. The inverse contrast-matching technique of small-angle neutron scattering enabled selective observation of KaiB in complex with the KaiC mutant with partial deuteration. It revealed a disk-shaped arrangement of the KaiB subunits on the outer surface of the KaiC C1 ring, which also serves as the interaction site for SasA, a histidine kinase that operates as a clock-output protein in the regulation of circadian transcription. These data suggest that cooperatively binding KaiB competes with SasA with respect to interaction with KaiC, thereby promoting the synergistic release of this clock-output protein from the circadian oscillator complex.
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