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Article

Direct interaction between KaiA and KaiB revealed by a site-directed spin labeling electron spin resonance analysis.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Mar 2010

Mutoh Risa, Mino Hiroyuki, Murakami Reiko, Uzumaki Tatsuya, Takabayashi Atsushi, Ishii Kentaro, Ishiura Masahiro

Abstract excerpt

In cyanobacteria, three clock proteins, KaiA, KaiB and KaiC, play essential roles in generating circadian oscillations. The interactions of these proteins change during the circadian cycle. Here, we demonstrated direct interaction between KaiA and KaiB using electron spin resonance spectroscopy. We prepared cystein (Cys)-substituted mutants of Thermosynechococcus elongatus KaiB, labeled specifically their Cys...

Topics

Bacterial Proteins
Circadian Rhythm Signaling Peptides and Proteins
Cysteine
Electron Spin Resonance Spectroscopy
Mutation
Protein Binding
Recombinant Proteins
Spin Labels
Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20113360
DOI: 10.1111/j.1365-2443.2009.01377.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-20113360-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Direct interaction between KaiA and KaiB revealed by a site-directed spin labeling electron spin resonance analysis.PMID 20113360Read ↗

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Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering.Semantic proximity Read ↗

Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC.Semantic proximity Read ↗

Protein-Protein Interactions in the Cyanobacterial Circadian Clock: Structure of KaiA Dimer in Complex with C-Terminal KaiC Peptides at 2.8 Å Resolution.Semantic proximity Read ↗

Two KaiA-binding domains of cyanobacterial circadian clock protein KaiC.Semantic proximity Read ↗

The roles of the dimeric and tetrameric structures of the clock protein KaiB in the generation of circadian oscillations in cyanobacteria.Semantic proximity Read ↗

Structures of KaiC circadian clock mutant proteins: a new phosphorylation site at T426 and mechanisms of kinase, ATPase and phosphatase.Semantic proximity Read ↗

Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria.Semantic proximity Read ↗

Dephosphorylation of the core clock protein KaiC in the cyanobacterial KaiABC circadian oscillator proceeds via an ATP synthase mechanism.Semantic proximity Read ↗

ATPase activity of KaiC determines the basic timing for circadian clock of cyanobacteria.Semantic proximity Read ↗

Tuning the circadian period of cyanobacteria up to 6.6 days by the single amino acid substitutions in KaiC.Semantic proximity Read ↗

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