PHOTOSYSTEM II SUBUNIT R Is Required for Efficient Binding of LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 to Photosystem II-Light-Harvesting Supercomplexes in Chlamydomonas reinhardtii1
PHOTOSYSTEM II SUBUNIT R Is Required for Efficient Binding of LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 to Photosystem II-Light-Harvesting Supercomplexes in Chlamydomonas reinhardtii1
复制标题
光系统II亚基R是莱茵衣藻中捕光复合体胁迫相关蛋白3与光系统II - 捕光超级复合体高效结合所必需的 1 注释：“1”如果在原文中有特殊含义，比如是参考文献标号等，需根据实际情况处理，这里暂按原文呈现。
DOI：
10.1104/pp.15.00094
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发表时间：
2015-02
期刊：
影响因子：
7.4
通讯作者：
Huidan Xue;Ryutaro Tokutsu;S. V. Bergner;M. Scholz;J. Minagawa;M. Hippler
中科院分区：
文献类型：
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作者：
Huidan Xue;Ryutaro Tokutsu;S. V. Bergner;M. Scholz;J. Minagawa;M. Hippler
莱茵衣藻有效的光到热耗散需要一个与应力相关的光收集复合体蛋白与光系统II和相关的光收集复合体II结合。在莱茵衣藻（Chlamydomonas reinhardtii）中，光收集复合体应力相关蛋白3 （LHCSR3）蛋白对过量吸收光能的高效能量依赖热耗散至关重要，并在功能上与光系统II-光收集复合体II （PSII-LHCII）超配合物相关。目前，LHCSR3如何与PSII-LHCII超复合体结合尚不清楚。在这项研究中，我们研究了PHOTOSYSTEM II亚基R （PSBR）在LHCSR3与PSII- lhcii超配合物结合中的作用。PSBR是PSII固有的跨膜亚基。下调PSBR表达降低了析氧效率和非光化学猝灭程度，影响了析氧复合物的稳定性以及PSII-LHCII-LHCSR3超复合物的形成。定量蛋白质组学显示，它的下调破坏了PSII-LHCII超复合体的稳定性，并强烈降低了LHCSR3与PSII-LHCII超复合体的结合。相反，PHOTOSYSTEM II亚基P缺失破坏了PHOTOSYSTEM II亚基Q结合的稳定性，但不影响PSBR和LHCSR3与PSII-LHCII的关联。综上所述，这些数据提供了明确的证据，表明PSBR是LHCSR3与PSII-LHCII超配合物稳定结合所必需的，并且对于持续强光下PSII-LHCII-LHCSR3超配合物的高效能量依赖猝灭和完整性至关重要。
Efficient light to heat dissipation in Chlamydomonas reinhardtii requires binding of a stress-related light-harvesting complex protein to photosystem II and associated light-harvesting complexes II. In Chlamydomonas reinhardtii, the LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 (LHCSR3) protein is crucial for efficient energy-dependent thermal dissipation of excess absorbed light energy and functionally associates with photosystem II-light-harvesting complex II (PSII-LHCII) supercomplexes. Currently, it is unknown how LHCSR3 binds to the PSII-LHCII supercomplex. In this study, we investigated the role of PHOTOSYSTEM II SUBUNIT R (PSBR) an intrinsic membrane-spanning PSII subunit, in the binding of LHCSR3 to PSII-LHCII supercomplexes. Down-regulation of PSBR expression diminished the efficiency of oxygen evolution and the extent of nonphotochemical quenching and had an impact on the stability of the oxygen-evolving complex as well as on PSII-LHCII-LHCSR3 supercomplex formation. Its down-regulation destabilized the PSII-LHCII supercomplex and strongly reduced the binding of LHCSR3 to PSII-LHCII supercomplexes, as revealed by quantitative proteomics. PHOTOSYSTEM II SUBUNIT P deletion, on the contrary, destabilized PHOTOSYSTEM II SUBUNIT Q binding but did not affect PSBR and LHCSR3 association with PSII-LHCII. In summary, these data provide clear evidence that PSBR is required for the stable binding of LHCSR3 to PSII-LHCII supercomplexes and is essential for efficient energy-dependent quenching and the integrity of the PSII-LHCII-LHCSR3 supercomplex under continuous high light.