Article
Loop-loop interactions regulate KaiA-stimulated KaiC phosphorylation in the cyanobacterial KaiABC circadian clock.
Biochemistry - 19 Feb 2013
Egli Martin, Pattanayek Rekha, Sheehan Jonathan H, Xu Yao, Mori Tetsuya, Smith Jarrod A, Johnson Carl H
Abstract excerpt
The Synechococcus elongatus KaiA, KaiB, and KaiC proteins in the presence of ATP generate a post-translational oscillator that runs in a temperature-compensated manner with a period of 24 h. KaiA dimer stimulates phosphorylation of KaiC hexamer at two sites per subunit, T432 and S431, and KaiB dimers antagonize KaiA action and induce KaiC subunit exchange. Neither the mechanism of KaiA-stimulated KaiC...
Topics
- Bacterial Proteins
- Circadian Clocks
- Circadian Rhythm Signaling Peptides and Proteins
- Crystallography, X-Ray
- Models, Molecular
- Molecular Dynamics Simulation
- Mutation
- Phosphorylation
- Protein Conformation
- Protein Multimerization