Journal
EMBO JOURNAL
Volume 22, Issue 9, Pages 2117-2126Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/cdg168
Keywords
circadian; clock; cyanobacteria; degradation; phosphorylation
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Funding
- NIGMS NIH HHS [GM67152, R01 GM067152, R37 GM067152] Funding Source: Medline
- NIMH NIH HHS [MH01179, K02 MH001179, R01 MH043836, MH43836] Funding Source: Medline
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Using model strains in which we ectopically express the cyanobacterial clock protein KaiC in cells from which the clock genes kaiA, kaiB and/or kaiC are deleted, we found that some features of circadian clocks in eukaryotic organisms are conserved in the clocks of prokaryotic cyanobacteria, but others are not. One unexpected difference is that the circadian autoregulatory feedback loop in cyanobacteria does not require specific clock gene promoters as it does in eukaryotes, because a heterologous promoter can functionally replace the kaiBC promoter. On the other hand, a similarity between eukaryotic clock proteins and the cyanobacterial KaiC protein is that KaiC is phosphorylated in vivo. The other essential clock proteins KaiA and KaiB modulate the status of KaiC phosphorylation; KaiA inhibits KaiC dephosphorylation and KaiB antagonizes this action of KaiA. Based upon an analysis of clock mutants, we conclude that the circadian period in cyanobacteria is determined by the phosphorylation status of KaiC and also by the degradation rate of KaiC. These observations are integrated into a model proposing rhythmic changes in chromosomal status.
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