The core circadian oscillator of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro by mixing the proteins KaiA, KaiB, and KaiC, resulting in oscillations in KaiC phosphorylation. The underlying mechanism of this biochemical oscillator has been elusive. Rust et al. (see the Perspective by Poon and Ferrell) now show that phosphorylation of KaiC at two residues is cyclically ordered and that the abundance of each phosphorylated form determines the phase of the oscillator. This sequential phosphorylation of KaiC, combined with negative feedback caused by one of the phosphorylation states, is sufficient to explain stable oscillation.
- Dissecting a Core Oscillator
The cycling of three protein components comprising the circadian clock in cyanobacteria is driven by a pattern of sequential phosphorylation that can be described mathematically.Permalink: