Project/Area Number |
63044047
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Research Category |
Grant-in-Aid for international Scientific Research
|
Allocation Type | Single-year Grants |
Section | Joint Research |
Research Institution | Tokyo Institute of Technology |
Principal Investigator |
OSHIMA Tairo Professor, Tokyo Institute of Technology, Departmemt of Life Science, 生命理工学部, 教授 (60167301)
|
Co-Investigator(Kenkyū-buntansha) |
ALLISON S. W. Professor, University of California, San Diego, Departmemt of Biochemistry, 生物化学科・サンジエゴ校, 教授
SCHAFER G. Professor, Medical University of Lubeck, Departmemt of Biochemistry, 医学部, 教授
OHNISHI T. Associate Professor, University of Philadelphia, School of Medicine, 生物化学・生物物理学科, 準教授
HOCHSTEIN L. Branch Chief, NASA Ames Research Center, Exobiology Division, エームス研究センター, 主任研究員
FRIEDMAN S. M. Professor, New York City University - Hunter College, Dept. of Biological Scienc, 生物学部・ハンター校, 教授
AZZI A. Professor, Bern University, Departmemt of Biochemistry, 医学部, 教授
北川 禎三 国立分子科学研究所, 室長 (40029955)
曽根 〓史 自治医科大学, 医学部, 助教授 (20049034)
YAMANAKA T. Professor, Tokyo Institute of Technology, Department of Life Science, 生命理工学部, 教授 (40028113)
吉田 賢右 東京工業大学, 生命理工学部, 教授 (90049073)
SONE H. Associate Professor, Jichi Medical School, Department of Biochemistry
KITAGAWA T. Chief, National Institute for Molecular Sciences
YOSHIDA M. Professor, Tokyo Institute of Technology, Department of Life Science
|
Project Period (FY) |
1988 – 1990
|
Project Status |
Completed (Fiscal Year 1990)
|
Budget Amount *help |
¥5,900,000 (Direct Cost: ¥5,900,000)
Fiscal Year 1990: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1989: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1988: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
Keywords | ATPases / Early biochemical evolution of life / Electron transport system / Cytochromes / Gene cloning and base sequences / Sequence homology |
Research Abstract |
1 Membrane-bound ATPases were solubilized and purified from Archaeo-bacterial cytoplasmic membranes, and genes encoding these ATPases were cloned and sequenced. It has been revealed that ATPases from vacuolar membranes in eukaryote cells resemble the Archaeo-bacterial ATPases in respect to inhibitor sensitivity, immunochemical reactivity, and sequence homology, and that these ATPases can be classified into a different family from F_1-ATPase of eubacteria and mitochondria.. Based on these observations. Archaeo-bacterial origin of vacuolar membranes has been proposed. 2 Terminal oxidases were solubilized from cytoplasmic membranes of an acidothermophilic archaebacteria, Sulfolobus acidocaldarius. Two heme a containing cytochromes were purified ; one is cytochrome aa_3 and oxidized quinones. The other has cytochrome c oxidase activity, but since cytochrome c is not present in either the cytoplasm or the membrane of the Archaeo-bacterial, the real substrate for this cytochrome remains to be solved in the future studies. Based on these observations, the presence of two independent electron transport chins in the Archaeo-bacterial membranes has been proposed. 3 An Archaeo-bacterial ferredoxine was purified from Sulfolobus acidocaldarius and crystallized. A preliminary study has been made on the crystallographic analysis of the iron-sulfur protein. Pyrophosphatase of the same microorganism was also purified and its enzymatic properties were investigated.
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