Study on the molecular basis for the regulation of redox metabolism network in plastids
| Project/Area Number |
13440240
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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 | Osaka University |
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Principal Investigator |
HASE Toshiharu Osaka University, Institute for Protein , Protein Research, Professor, たんぱく質研究所, 教授 (00127276)
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| Co-Investigator(Kenkyū-buntansha) |
ARIGA Yoko Osaka University, Institute for Protein Protein Research, Instructor, たんぱく質研究所, 助手 (60255429)
KUSUNOKI Masami Osaka University, Institute for Protein Protein Research, Associate Professor, たんぱく質研究所, 助教授 (90135749)
藤田 祐一 大阪大学, たんぱく質研究所, 助手 (80222264)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥16,800,000 (Direct Cost: ¥16,800,000)
Fiscal Year 2002: ¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 2001: ¥12,700,000 (Direct Cost: ¥12,700,000)
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| Keywords | plastid / redox metabolism / ferredoxin / ferredoxin:NADP reductase / sulfite reductase / glutamate synhtase / フェレドキシン:NADP還元酵素 |
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| Research Abstract |
Autotrophic capacity of plants depends on a series of redox of redox metabolisms. An electron carrir protein, ferredoxin (Fd) and Fd-dependent enzymes function in combination as a molecular machinery for such metabolisms. The process of electron partitioning via Fd to various enzymes within plastids is crucial for photosynthetic activity and elucidation of its molecular mechanism is the main aim of this study. Following results has been obtained.
1) X-ray crystsl structure of an electron transfer complex of root Ed and Fd:NADP+ reductase has been determied and this structure is found to be different from that of lesf counterpart.
2) Electron transfer between sulfite reductase and Fd was investigate using wild type ans their mutant molecules and redox potential of Fd was found to be important for activity and substrate specificity of sulfite reductase. X-ray crystal analysis of this enzyme is now ongoing.
3) Site diredted mutagenesis study of Fd-dependent glutamate synthase was done. Amino acids necessary for the activity of he amidotransferae domain of this enzyme were identified.
4) Based on the total total genome information of Arabidopsis, 4 Fd isoprotiens were prepared and purified by reconbinant technique. Their abilities in the electron transfer to photosystem. I, Fd:NADP+ reductase and sulfite reductase were significantly different and physiological differentiation of their role was elucidated. Now proteins which interact with each Fd isoprotein are under investigation.
5) A cyanobacterial mutant lacking Fd-dependent glutamate synthase exhibits unbalancing of carbon and nitrogen assimilation probably due to disturbance of partitioning of reducing equivalent. In response to this unbalancing the expression of glutamate synthase gene was up and down-regulated. We could monitor this gene expression by reporterassay syatem.
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Report
(3 results)
Research Products
(15 results)
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[Publications] Teshima,K., Fujita,S., Hirose,S., Nishiyama,D., Kurisu,G., Kusunoki,M., Kimata-Ariga,Y., and Hase,T.: "A ferredoxin Arg-Glu pair important for efficient electron transfer between ferredoxin and ferredoxin-NADP^+ reductase"FEBS Lett.. in press. (2003)
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[Publications] Maeda,M., Hamada,D., Hoshino,M., Onda,Y., Hase,T., and Goto,Y.: "Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin-NADP^+ reductase with residual NADP^+ binding domain"J. Biol. Chem.. 277. 17101-17107 (2002)
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