期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 284, 期 37, 页码 25343-25352出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.007740
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [20570039, 18208008]
- Wesco Science Promotion Foundation
- Ryobi Foundation
- Ministry of Education, Youth and Sports of the Czech Republic [MSM 6198959215]
- Japan Society for the Promotion of Science
- Department of Biotechnology, India
- Grants-in-Aid for Scientific Research [20570039, 18208008] Funding Source: KAKEN
Photosystem II is vulnerable to light damage. The reaction center-binding D1 protein is impaired during excessive illumination and is degraded and removed from photosystem II. Using isolated spinach thylakoids, we investigated the relationship between light-induced unstacking of thylakoids and damage to the D1 protein. Under light stress, thylakoids were expected to become unstacked so that the photodamaged photosystem II complexes in the grana and the proteases could move on the thylakoids for repair. Excessive light induced irreversible unstacking of thylakoids. By comparing the effects of light stress on stacked and unstacked thylakoids, photoinhibition of photosystem II was found to be more prominent in stacked thylakoids than in unstacked thylakoids. In accordance with this finding, EPR spin trapping measurements demonstrated higher production of hydroxyl radicals in stacked thylakoids than in unstacked thylakoids. We propose that unstacking of thylakoids has a crucial role in avoiding further damage to the D1 protein and facilitating degradation of the photodamaged D1 protein under light stress.
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