| Project/Area Number |
09274103
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas (A)
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| Allocation Type | Single-year Grants |
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
SATO Fumihiko Kyoto University, Graduate School of Biostudies, Professor, 大学院・生命科学研究科, 教授 (10127087)
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| Co-Investigator(Kenkyū-buntansha) |
HASE Toshiharu Osaka University, Institute for Protein Research, Professor, 蛋白質研究所, 教授 (00127276)
OMATA Tatsuo Nagoya University, Graduate School of Bioagricultural Sciences, Professor, 大学院・生命農学研究科, 教授 (50175270)
SUGITA Mamoru Nagoya University, Center for Gene Research, Professor, 遺伝子実験施設, 教授 (70154474)
NISHIMURA Mikio Okazaki National Research Institutes, National Institute for Basic Biology, Professor, 基礎生物学研究所, 教授 (80093061)
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| Project Period (FY) |
1997 – 2000
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| Keywords | Chloroplastic DNA-binding protease / Chloroplastic RNA-binding protein / Chloroplast development and plant growth / PII and NtcA in C / N metabolism / Redox regulation in plastid / Fd / FNR protein interaction / Light regulation of alternative splicing / Trans-acting factors in alternative splicing |
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| Research Abstract |
1. A novel chloroplast nucleoid DNA-binding protein with protease activity, CND41, has been identified and its multiple functions in Rubisco degradation during senescence, chloroplast development in meristem, growth regulation via gibberellin biosynthesis and so on were characterized.
2. The RNA-stablizing activity of chloroplastic RNA-binding proteins (cpRNP) on stroma-accumulating transcripts was found and the target RNA species were identified using chloroplast DNA-microarray.
3. The mechanism of electron transfer around Photosystem I through specific Fd molecules for mesophyll and bundle sheath cells in C4 maize plants was clarified to control the carbon/nitrogen metabolism. Three dimensional structure of Fd/FNR complex was resolved to declare the molecular mechanism of the regulation of electron transfer.
4. Using cyanobacterium as a model, the molecular mechanism of the control of carbon/nitrogen metabolism was clarified ; 2-oxoglutarate was shown to be essential for transcriptional activation by NtcA (the global nitrogen regulator) of the N assimilation genes ; The regulatory domain of the nitrate transporter, involved in downregulation of the transport activity under N-replete conditions, was identified and shown to control the transport activity in concert with PII (the glnB gene product).
5. Regulation of subcellular localization of peroxisomal hydroxypyruvate reductase and chloroplastic ascorbate peroxidase by alternative splicing was established and the trans-acting factor involved in the splicing was isolated. Several mutants with defects in beta-oxidation pathway have been isolated and the mechanism in lipid degradation in glyoxisome has been considerably clarified.
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