Volume 09, No.5
目次 / Table of Contents
September issue 2004
1. SPring-8の現状／PRESENT STATUS OF SPring-8
2004B 利用研究課題選定委員会を終えて
Report of the Proposal Review Committee on the 14th Public Research Term 2004B
Report of the Proposal Review Committee on the 14th Public Research Term 2004B
東京工業大学 応用セラミックス研究所 Materials and Structures Laboratory, Tokyo Institute of Technology
2. 最近の研究から／FROM LATEST RESEARCH
[1]名古屋大学 遺伝子実験施設 Center for Gene Research, Nagoya University、[2]京都大学大学院 薬学研究科 Graduate School of Pharmaceutical Sciences, Kyoto University、[3]京都大学大学院 薬学研究科 Graduate School of Pharmaceutical Sciences, Kyoto University、[4]名古屋大学 遺伝子実験施設 Center for Gene Research, Nagoya University
- Abstract
- KaiA, KaiB, and KaiC constitute the circadian clock machinery in cyanobacteria. KaiA activates kaiBC expression while KaiC represses it. Here we demonstrated that KaiA is composed of three functional domains : the N-terminal amplitude-amplifier domain, the central period-adjuster domain, and the C-terminal clock-oscillator domain. The C-terminal domain is responsible for dimer formation, binding to KaiC, enhancing KaiC phosphorylation, and generating circadian oscillations. The 1.8 Å X-ray crystal structure of the C-terminal clock-oscillator domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 shows that residue His270, located at the center of a KaiA dimer concavity, is essential to KaiA function. KaiA binding to KaiC likely occurs via the concave surface. Based on the structure, we could predict the structural roles of the residues that affected circadian oscillations.
3. 研究会等報告／WORKSHOP AND COMMITTEE REPORT
兵庫県立大学大学院 物質理学研究科 Graduate School of Material Science, University of Hyogo
研究成果報告会 プログラム委員会 Program Committee, Meeting on the Results of Research Activities
（独）理化学研究所 播磨研究所 研究推進部 Research Promotion Division, Harima Institute, RIKEN
4. 告知板／ANNOUNCEMENTS
その他／MISC
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