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Article

A novel allele of kaiA shortens the circadian period and strengthens interaction of oscillator components in the cyanobacterium Synechococcus elongatus PCC 7942.

Journal of bacteriology - 1 Jul 2009

Chen You, Kim Yong-Ick, Mackey Shannon R, Holtman C Kay, Liwang Andy, Golden Susan S

Abstract excerpt

The basic circadian oscillator of the unicellular fresh water cyanobacterium Synechococcus elongatus PCC 7942, the model organism for cyanobacterial circadian clocks, consists of only three protein components: KaiA, KaiB, and KaiC. These proteins, all of which are homomultimers, periodically interact to form large protein complexes with stoichiometries that depend on the phosphorylation state of KaiC. KaiA...

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Share to Bacterial Proteins
Share to Circadian Rhythm

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19395479
DOI: 10.1128/JB.00334-09
PMCID: PMC2698500

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

A novel allele of kaiA shortens the circadian period and strengthens interaction of oscillator components in the cyanobacterium Synechococcus elongatus PCC 7942.PMID 19395479Read ↗

Mutations in KaiA, a clock protein, extend the period of circadian rhythm in the cyanobacterium Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

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

KaiA-stimulated KaiC phosphorylation in circadian timing loops in cyanobacteria.Semantic proximity Read ↗

Analysis of KaiA-KaiC protein interactions in the cyano-bacterial circadian clock using hybrid structural methods.Semantic proximity Read ↗

Circadian rhythms in the synthesis and degradation of a master clock protein KaiC 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 ↗

Two KaiA-binding domains of cyanobacterial circadian clock protein 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 ↗

CikA, a bacteriophytochrome that resets the cyanobacterial circadian clock.Semantic proximity Read ↗

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

Diversity of KaiC-based timing systems in marine Cyanobacteria.Semantic proximity Read ↗

Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro.Semantic proximity Read ↗

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