Abstract
KaiC is the central pacemaker of the circadian clock system in cyanobacteria and forms the core in the hetero-multimeric complexes, such as KaiB-KaiC and KaiA-KaiB-KaiC. Although the formation process and structure of the binary and ternary complexes have been studied extensively, their disassembly dynamics have remained elusive. In this study, we constructed an experimental system to directly measure the autonomous disassembly of the KaiB-KaiC complex under the condition where the dissociated KaiB cannot reassociate with KaiC. At 30°C, the dephosphorylated KaiB-KaiC complex disassembled with an apparent rate of 2.1±0.3 d(-1), which was approximately twice the circadian frequency. Our present analysis using a series of KaiC mutants revealed that the apparent disassembly rate correlates with the frequency of the KaiC phosphorylation cycle in the presence of KaiA and KaiB and is robustly temperature-compensated with a Q (10) value of 1.05±0.20. The autonomous cancellation of the interactions stabilizing the KaiB-KaiC interface is one of the important phenomena that provide a link between the molecular-scale and system-scale properties.