Project/Area Number |
09640795
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
生物形態・構造
|
Research Institution | Nippon Sport Science University |
Principal Investigator |
OSAFUNE Tetsuaki Nippon Sport Science Univ.Dept.of Life Science, Professor., 体育学部, 教授 (70074630)
|
Co-Investigator(Kenkyū-buntansha) |
OHKI Kaori Fukui Prefectural Univ., Dept.of Bioscience, Professor., 生物資源学部, 教授 (90101104)
|
Project Period (FY) |
1997 – 2000
|
Project Status |
Completed (Fiscal Year 2000)
|
Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2000: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1999: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1998: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1997: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
Keywords | Euglena / LHCP II / RuBisco / COS / RuBisCO / ゴルジ装置 / 塩化カドミウム / LHCP II / 免疫電顕法 / ユ-グレナ / 葉緑体形成過程 |
Research Abstract |
Precursors to the Euglena chlorophyll a/b binding protein (pLHCPII) and small subunit of ribulose-bis-phosphate carboxylase (pSSU) are transported in vesicles from ER to Golgi to chloroplast. Immunoelectron microscopy (IM) localizes SSU and LHCPII in greening cells to a membranous cytoplasmic osmiophilic structure (COS), the Golgi and chloroplast but never the nucleus or cytoplasm. Euglena cultured in the dark without aeration accumulate lipid. Upon aeration, lipid decreases, SSU accumulates and proplastids expand with limited prothylakoid formation. IM localizes SSU to the nucleus, COS, vacuolar structures and developing plastids of dark aerated cells. 15 C blocks Golgi to chloroplast transport inhibiting light induced chloroplast development and LHCPII accumulation. IM localizes LHCPII to the nucleus, COS, Golgi and plastids of 15 C cells. Western blotting demonstrates that pLHCPII levels are identical at 15 and 26 C while mature LHCPII accumulates slower and to lower levels at 15 C.Taken together, these experiments suggest that nuclear localization of chloroplast proteins is associated with disruption of normal plastid development. Chloroplast proteins are localized to the nucleus either by vesicle mistargeting or as is more likely through disruption of chloroplast integrity, release of chloroplast proteins to the cytoplasm and their subsequent diffusion into the nuclear compartment.
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