Structural transition of clock protein complex induced by change of phosphorylation state
Every life on the earth has a circadian clock, which is a biological oscillator with 24-hrs period. A circadian clock in cyanobacteria is the simplest and suitable one for research. This clock consists of only three proteins, KaiA, KaiB and KaiC, and, in vitro, display ATP dependent complex-formation and dissociation with a 24-hour period. It has been clarified that the particular complexes are formed depending upon the phosphorylation state of KaiC. Therefore, determining the correlation between the structure of complex and KaiC phosphorylation level is crucial to understand the mechanism of clock oscillation. Recently, in the higher phosphorylation state of KaiC, KaiCB complex absorbs twelve KaiAs and forms KaiCBA complex: it is supposed to induce dephosphorylation of KaiC. However, the complex was obtained under the extrem condition. Therefore, there are questions that "“Does KaiCB complex really absorb KaiA under the native condition?"” and "“If it does, is the complex (KaiCB+12KaiA) produced?”". The aim of this proposal is to reveal the formation process of the KaiCBA complexes by using size-exculsion chromatgraphy and iCM-SANS (SEC-iCM-SANS) in combination.
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Masaaki Sugiyama; INOUE Rintaro; MARTEL Anne; PORCAR Lionel; SATO Nobuhiro; TOMINAGA Taiki; VIGILD Martin and Rina Yogo. (2018). Structural transition of clock protein complex induced by change of phosphorylation state. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-938
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