| Project/Area Number |
13440238
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
植物生理
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
HISABORI Toru CHEMICAL RESOURCES LABORATORY, TOKYO INSTITUTE OF TECHONOLOGY, ASSOCIATE PROFESSOR, 資源化学研究所, 助教授 (40181094)
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| Co-Investigator(Kenkyū-buntansha) |
YOSHIDA Masasuke CHEMICAL RESOURCES LABORATORY, TOKYO INSTITUTE OF TECHONOLOGY, PROFESSOR, 資源化学研究所, 教授 (90049073)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥12,900,000 (Direct Cost: ¥12,900,000)
Fiscal Year 2003: ¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2002: ¥4,500,000 (Direct Cost: ¥4,500,000)
Fiscal Year 2001: ¥5,100,000 (Direct Cost: ¥5,100,000)
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| Keywords | SWITCH REGION / γSUBUNIT / ATP SYNTHASE / CHLOROPLAST / REDOX REGULATION / εSUBUNIT |
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| Research Abstract |
In this project, we intended to understand the redox regulation of chloroplast ATP synthase at the molecular level. For these three research years, we obtained the several important findings as follows:
A.The switch region from the γ subunit of the redox-sensitive chloroplast F1 was introduced into the bacterial F1 and the redox switching of the rotation was revealed. We revealed that the suppressed enzymatic activity of the oxidized Fl was characterized by more frequent long pauses in the rotation behaviour.
B.The regulatory function of the γ and ε subunits of chloroplast ATP synthase was studied using the membrane integrated chimeric complex. We concluded that the interaction between these subunits is important for the redox regulation of FoF1 complex by the γ subunit, and a certain structural matching between these regulatory subunits and the catalytic core of the enzyme must be required to confer the redox regulation mechanism to the bacterial FoF1.
C.The sensitivity against tentoxin, the specific inhibitor peptide for the chioroplast F1, was conferred to the bacteria Fl by a single amino acid substitution based on the three dimensional structure analysis. Then the rotation of this mutant Fl was investigated in the presence of this inhibitor. The change of the pauses induced by the inhibitor was revealed.
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