| Project/Area Number |
17207001
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Genetics/Genome dynamics
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| Research Institution | Nagoya University |
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Principal Investigator |
ISHIURA Masahiro Nagoya University, Cenhr for Gene Reseamh, Professor (20132730)
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| Co-Investigator(Kenkyū-buntansha) |
IHARA Kunio Nagoya University, Center for Gene Reseamh.Reseamh, Assistant Professor (90223297)
ITO Sigeru Nagoya University, Graduate Schoolof Science, Professor (40108634)
NAMBA Keiichi Osaka University, Graduate SclnolofFrontierFrience, Professor, 教授 (30346142)
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| Project Period (FY) |
2005 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥51,610,000 (Direct Cost: ¥39,700,000、Indirect Cost: ¥11,910,000)
Fiscal Year 2007: ¥13,520,000 (Direct Cost: ¥10,400,000、Indirect Cost: ¥3,120,000)
Fiscal Year 2006: ¥13,520,000 (Direct Cost: ¥10,400,000、Indirect Cost: ¥3,120,000)
Fiscal Year 2005: ¥24,570,000 (Direct Cost: ¥18,900,000、Indirect Cost: ¥5,670,000)
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| Keywords | Biological clock / Clock gene / KaiB / KaiC / ATPase / Pex / Cyanobacteria / Chlamydomonas / 時計タンパク質 / ATPase / 概日リズム / Kaiタンパク質 / シロイヌナズナ / 分子装置 / タンパク質間相互作用 / X線結晶構造解析 / 原子構造 |
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| Research Abstract |
We developed two kinds of automated bioluminescence-monitoring apparatuses and the bioluminescence rhythm-analyzing program RAP.
In cyanobacteria, we established the followings : 1)The N-terminal domain of clock protein KaiC is involved in the hexamerization of KaiC, and the C-terminal domain is involved in the inter-subunit phosphorylation of kaiC.2)KaiC has extremely weak ATPase activity, and the activity is enhanced by KaiA and is repressed by the phosphorylation of KaiC. Both the N-terminal and C-terminal domain proteins of KaiC have ATPase activity. KaiC ATPase activity is temperature-compensated, but the lack of phosphorylation sites in KaiC results in the loss of the temperature compensation.3)We determined the crystal structure of KaiB. Based on the atomic structure, we predicted important substructures and functional residues of KaiB that are involved in the clock oscillation of the clock machinery and confirmed their importance.4)We also determined the crystal structure of Pex, which is one of major components of the circadian input pathway of light. Based on the atomic structure, we predicted the functional residues of Pex that are involved in the interaction with DNA and confirmed their importance.5)Using DNA microarrays, we identified circadian-regulated genes and clarified their expression patterns.
In Chlamydomonas, we developed a bioluminescence-rhythm-monitoring system of chloroplasts, isolated various types of rhythm mutants, and then identified clock genes and clock-related genes. Some of the clock genes share common motifs with higher plant clock genes, and others are specific to Chlamydomonas.
In Arabidopsis, we cloned "a true clock gene" in the higher plant, PHYTOCLOCK 1.
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