Ontology highlight
ABSTRACT:
SUBMITTER: Chang YG
PROVIDER: S-EPMC3479483 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20120911 42
The oscillator of the circadian clock of cyanobacteria is composed of three proteins, KaiA, KaiB, and KaiC, which together generate a self-sustained ∼24-h rhythm of phosphorylation of KaiC. The mechanism propelling this oscillator has remained elusive, however. We show that stacking interactions between the CI and CII rings of KaiC drive the transition from the phosphorylation-specific KaiC-KaiA interaction to the dephosphorylation-specific KaiC-KaiB interaction. We have identified the KaiB-bind ...[more]