Study on the molecular mechanism of D1 protein aggregation in photosystem II under light and heat stresses
| Project/Area Number |
20570039
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Plant molecular biology/Plant physiology
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| Research Institution | Okayama University |
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Principal Investigator |
YAMAMOTO Yasushi Okayama University, 大学院・自然科学研究科, 教授 (40091251)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2010: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2009: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2008: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 光化学系II / D1タンパク質 / 光ストレス / 熱ストレス / FtsHプロテアーゼ / チラコイド / 活性酸素 / 光化学系IIの品質管理 / Ftshプロテアーゼ / 光化学系IIの晶質管理 / 品質管理 / チラコイド膜 / 光合成 / ホウレンソウ / 脂質過酸化 / unstacking / D1タンパク質分解 |
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| Research Abstract |
The results of our 3 years' research activity are summarized as follows : (1) Under light and heat stresses, lipid peroxidation and the subsequent production of reactive oxygen species take place, which become one of the causes for oxidative damage, aggregation and degradation of the D1 protein. (2) To prevent further damage to the D1 protein under light stess, the thylakoid membranes show structural changes including membrane unstacking. (3) When the photosystem II complexes in the grana are photodamaged under high light, subunits of metalloprotease FtsH forms hexamers at the grana, probably at the grana margin, and carry out degradation of the damaged D1 protein.
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Report
(4 results)
Research Products
(62 results)
