| Project/Area Number |
12440228
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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 | NAGOYA UNIVERSITY |
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Principal Investigator |
OGAWA Teruo NAGOYA UNIVERSITY, BIOSCIENCE CENTER, PROFESSOR, 生物分子応答研究センター, 教授 (80087593)
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| Co-Investigator(Kenkyū-buntansha) |
OMATA Tatsuo NAGOYA UNIVERSITY GRADUATE COURSE OF BIOAGRICULTURAL SCIENCES, PROFESSOR, 生命農学研究科, 教授 (50175270)
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| Project Period (FY) |
2000 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥11,000,000 (Direct Cost: ¥11,000,000)
Fiscal Year 2002: ¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 2001: ¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2000: ¥3,900,000 (Direct Cost: ¥3,900,000)
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| Keywords | CO_2-concentrating mechanism / CO_2 pump / NADPH dehydrogenase / Bicarbonate transporter / SbtA-dependent type / Cmp-dependent type / NdhD3-dependent type / NdhD4-dependent type / ndh遺伝子 / NAD(P)Hデヒドロゲナーゼ / らん藻 / sbtA / HCO_3^-輸送 / cmpA / cbbR / 変異株 / cmpオペロン |
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| Research Abstract |
We have identified two CO_2-uptake systems, one constitutive dependent on NdhD3/NdhF3/CupA(Sll 1734) and one low-CO_2-inducible dependent on NdhD4/NdhF4/CupB(Slr 1302), and two types of HCO_3^- transporters, an ABC-type transporter encoded by cmp operon and a novel sodium-dependent transporter encoded by slr 1512 (sbtA) that plays a central role in HCO_3^- uptake in the cyanobacterium Synechocystis sp, strain PCC 6803. Mutants impaired for one of these 4 inorganic carbon-acquisition systems did not show mutant phenotype. Mutants inactivated for both CO_2-uptake systems were unable to grow at pH 7.0 in air although they grew normally at pH 9.0 in air. Additional inactivation of the SbtA-type HCO_3^- transporter abolished the growth at pH 9.0 in air. Using the antibody raised against SbtA, we have shown that SbtA is localized in the cytoplasmic membrane. Immunoprecipitation using this antibody revealed that a protein of about 10 kDa was coprecipitated with SbtA. Amino-acid sequencing revealed that this protein the product of slr 1513 (named as sbtB) cotranscribed with sbtA.
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