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Light-Harvesting Complex Stress-Related Proteins Catalyze Excess Energy Dissipation in Both Photosystems of Physcomitrella patens

机译:采光复杂的应激相关蛋白催化小立碗藓两个光系统中的过多能量耗散

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摘要

Two LHC-like proteins, Photosystem II Subunit S (PSBS) and Light-Harvesting Complex Stress-Related (LHCSR), are essential for triggering excess energy dissipation in chloroplasts of vascular plants and green algae, respectively. The mechanism of quenching was studied in Physcomitrella patens, an early divergent streptophyta (including green algae and land plants) in which both proteins are active. PSBS was localized in grana together with photosystem II (PSII), but LHCSR was located mainly in stroma-exposed membranes together with photosystem I (PSI), and its distribution did not change upon high-light treatment. The quenched conformation can be preserved by rapidly freezing the high-light-treated tissues in liquid nitrogen. When using green fluorescent protein as an internal standard, 77K fluorescence emission spectra on isolated chloroplasts allowed for independent assessment of PSI and PSII fluorescence yield. Results showed that both photosystems underwent quenching upon high-light treatment in the wild type in contrast to mutants depleted of LHCSR, which lacked PSI quenching. Due to the contribution of LHCII, P. patens had a PSI antenna size twice as large with respect to higher plants. Thus, LHCII, which is highly abundant in stroma membranes, appears to be the target of quenching by LHCSR.
机译:两种LHC样蛋白,分别是Photosystem II亚基S(PSBS)和与光采复应力有关(LHCSR),对于触发维管植物和绿藻的叶绿体中的过多能量耗散至关重要。猝灭的机理在Physcomitrella patens(一种早期分化的链霉菌(包括绿藻和陆地植物))中进行了研究,其中两种蛋白质均具有活性。 PSBS与光系统II(PSII)一起定位在格兰娜中,但是LHCSR主要与光系统I(PSI)一起位于基质暴露的膜中,并且在高光处理下其分布没有变化。淬灭的构象可以通过在液氮中快速冷冻经高光处理的组织来保存。当使用绿色荧光蛋白作为内标时,分离的叶绿体上的77K荧光发射光谱可独立评估PSI和PSII荧光产量。结果表明,与缺乏LSISR的缺少PSI淬灭作用的突变体相比,野生型中的两个光系统都经过了高光处理后淬灭。由于LHCII的贡献,P。patens的PSI天线尺寸是高等植物的两倍。因此,在基质膜中高度丰富的LHCII似乎是通过LHCSR淬灭的靶标。

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