Structural study on clock protein: Relation between phosphorylation and its allosteric effect on the structure
Biological clock regulates many physiological activities and the wrong clock induces serious diseases. Therefore, to understand the biological clock system is remarkably important not only for a fundamental biology but also medical point of view. 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 display ATP dependent complex-formation and dissociation with a 24-hour period. Through intensive researches in the last few decades, it has been clarified that KaiC controls the clock phase by oscillating its phosphorylation state, and KaiA and KaiB modulate KaICs phosphorylation activity. However, the shortage of structural knowledge hinders fully understanding of this clock mechanism. In this proposal, using the phosphorylation-state-mimicking mutants and also conducting SANS by utilizing its features, contrast matching, 75%-deuteration and partial domatin-deuteration, we will reveal the relation between the phosphorylation state of KaiC and its allosteric effect on the structures of KaiC and its complex with KaiB.
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Masaaki Sugiyama; INOUE Rintaro; MARTEL Anne; Yuuya NAGATA; PORCAR Lionel; YAGI Hirokazu; YUNOKI YASUHIRO and ZACCAI Joseph. (2015). Structural study on clock protein: Relation between phosphorylation and its allosteric effect on the structure. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-838
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