Irreversible photoinhibition of photosystem II is caused by exposure of Synechocystis cells to strong light for a prolonged period

被引:17
|
作者
Allakhverdiev, SI
Tsvetkova, N
Mohanty, P
Szalontai, B
Moon, BY
Debreczeny, M
Murata, N [1 ]
机构
[1] Natl Inst Basic Biol, Okazaki, Aichi 4448585, Japan
[2] Russian Acad Sci, Inst Basic Biol Problems, Pushchino 142290, Moscow Region, Russia
[3] Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA
[4] Jawaharlal Nehru Univ, New Delhi 110067, India
[5] Univ Indore, Indore 452017, India
[6] Hungarian Acad Sci, Inst Biophys, Szeged, Hungary
[7] Inje Univ, Dept Biol, Gimhae, South Korea
[8] Grad Univ Adv Studies, Sch Life Sci, Dept Mol Biomech, Okazaki, Aichi 4448585, Japan
来源
基金
匈牙利科学研究基金会; 日本学术振兴会;
关键词
photodamage; photosystem II; D1; protein; Synechocystis;
D O I
10.1016/j.bbabio.2005.05.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Irreversible photoinhibition of photosystem II (PSII) occurred when Synechocystis sp. PCC 6803 cells were exposed to very strong light for a prolonged period. When wild-type cells were illuminated at 20 degrees C for 2 h with light at an intensity of 2,500 mu mol photons m(-2) s(-1), the oxygen-evolving activity of PSII was almost entirely and irreversibly lost, whereas the photochemical reaction center in PSII was inactivated only reversibly. The extent of irreversible photoinhibition was enhanced at lower temperatures and by the genetically engineered rigidification of membrane lipids. Western and Northern blotting demonstrated that, after cells had undergone irreversible photoinhibition, the precursor to D1 protein in PSII was synthesized but not processed properly. These observations may suggest that exposure of Synechocystis cells to strong light results in the irreversible photoinhibition of the oxygen-evolving activity of PSII via impairment of the processing of pre-D1 and that this effect of strong light is enhanced by the rigidification of membrane lipids. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:342 / 351
页数:10
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