Quality control of PSII: behavior of PSII in the highly crowded grana thylakoids under excessive light.

Quality control of PSII: behavior of PSII in the highly crowded grana thylakoids under excessive light.
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DOI:
10.1093/pcp/pcu043
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发表时间:
2014-07
影响因子:
4.9
通讯作者:
Ishikawa Y
Ishikawa Y
中科院分区:
生物学2区
文献类型:
--
作者:
Yamamoto Y;Kai S;Ohnishi A;Tsumura N;Ishikawa T;Hori H;Morita N;Ishikawa Y

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高等植物叶绿体的基粒类囊体中充满了PSII和与之相关的捕光复合物(LHCIIs)。它们构成超复合体,并且经常在基粒中形成半晶体阵列。拥挤的条件下的基粒可能是必要的激发能量的有效捕获LHCII在弱光下,但它可能会阻碍适当的运动LHCII的可逆聚集LHCII在Chl荧光的能量依赖性淬灭在中等高的光。当类囊体被极强的光照射时,PSII的反应中心结合D1蛋白被光损伤,并且受损的蛋白质迁移到基粒边缘进行降解和随后的修复。在中等和极端的强光条件下,类囊体膜的流动性是至关重要的。本文首先综述了光保护过程的研究进展,然后讨论了在过量光照下,光系统II的光保护作用与膜流动性和基粒中蛋白质复合物的迁移率的变化。我们推测,LHCII的可逆聚集,这是必要的,以避免在中度强光下的光应激,和快速营业额的光损伤的D1蛋白在极高的光下受到威胁的不可逆的蛋白质聚集诱导的活性氧在光化学反应。
The grana thylakoids of higher plant chloroplasts are crowded with PSII and the associated light-harvesting complexes (LHCIIs). They constitute supercomplexes, and often form semi-crystalline arrays in the grana. The crowded condition of the grana may be necessary for efficient trapping of excitation energy by LHCII under weak light, but it might hinder proper movement of LHCII necessary for reversible aggregation of LHCII in the energy-dependent quenching of Chl fluorescence under moderate high light. When the thylakoids are illuminated with extreme high light, the reaction center-binding D1 protein of PSII is photodamaged, and the damaged protein migrates to the grana margins for degradation and subsequent repair. In both moderate and extreme high-light conditions, fluidity of the thylakoid membrane is crucial. In this review, we first provide an overview of photoprotective processes, then discuss changes in membrane fluidity and mobility of the protein complexes in the grana under excessive light, which are closely associated with photoprotection of PSII. We hypothesize that reversible aggregation of LHCII, which is necessary to avoid light stress under moderate high light, and swift turnover of the photodamaged D1 protein under extreme high light are threatened by irreversible protein aggregation induced by reactive oxygen species in photochemical reactions.
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