Division of Biological Science, Graduate School of Science, Nagoya University and CREST, Japan Science and Technology Agency (JST), Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
FEBS Lett. 2010 Mar 5;584(5):898-902. doi: 10.1016/j.febslet.2010.01.016. Epub 2010 Jan 16.
Biochemical circadian oscillation of KaiC phosphorylation, by mixing three Kai proteins and ATP, has been proven to be the central oscillator of the cyanobacterial circadian clock. In vivo, the intracellular levels of KaiB and KaiC oscillate in a circadian fashion. By scrutinizing KaiC phosphorylation rhythm in a wide range of Kai protein concentrations, KaiA and KaiB were found to be "parameter-tuning" and "state-switching" regulators of KaiC phosphorylation rhythm, respectively. Our results also suggest a possible entrainment mechanism of the cellular circadian clock with the circadian variation of intracellular levels of Kai proteins.
凯克磷酸化的生化昼夜振荡，通过混合三种凯蛋白和 ATP，已被证明是蓝藻生物钟的中央振荡器。在体内，凯 B 和凯 C 的细胞内水平呈昼夜节律波动。通过在广泛的凯蛋白浓度范围内仔细研究凯 C 的磷酸化节律，发现 KaiA 和 KaiB 分别是 KaiC 磷酸化节律的“参数调谐”和“状态转换”调节剂。我们的结果还表明，细胞生物钟可能存在一种与凯蛋白细胞内水平昼夜变化相适应的机制。
