Quality control of photosystem II: impact of light and heat stresses
Quality control of photosystem II: impact of light and heat stresses
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DOI：
10.1007/s11120-008-9372-4
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发表时间：
2008-10
影响因子：
3.7
通讯作者：
Yasusi Yamamoto;Ryota Aminaka;M. Yoshioka;M. Khatoon;K. Komayama;Daichi Takenaka;Amu Yamashita;
中科院分区：
文献类型：
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作者：
Yasusi Yamamoto;Ryota Aminaka;M. Yoshioka;M. Khatoon;K. Komayama;Daichi Takenaka;Amu Yamashita;
光系统II易受各种非生物胁迫，如强可见光和热。在这两种胁迫下，损伤似乎都是由活性氧触发的，而最关键的损伤发生在反应中心结合的D1蛋白上。近年来，在识别参与光或热损伤D1蛋白降解的蛋白酶，atp依赖性金属蛋白酶FtsH方面取得了进展。另一个重要的结果是发现受损的D1蛋白与附近的多肽聚集，如D2蛋白和天线叶绿素结合蛋白CP43。D1蛋白的降解和聚集同时发生，但两者之间的关系尚不清楚。我们认为，D1蛋白的磷酸化和去磷酸化，以及外源性PsbO蛋白与光系统II的结合，在将受损的D1蛋白导向两个可选途径中发挥调节作用。
Photosystem II is vulnerable to various abiotic stresses such as strong visible light and heat. Under both stresses, the damage seems to be triggered by reactive oxygen species, and the most critical damage occurs in the reaction center-binding D1 protein. Recent progress has been made in identifying the protease involved in the degradation of the photo- or heat-damaged D1 protein, the ATP-dependent metalloprotease FtsH. Another important result has been the discovery that the damaged D1 protein aggregates with nearby polypeptides such as the D2 protein and the antenna chlorophyll-binding protein CP43. The degradation and aggregation of the D1 protein occur simultaneously, but the relationship between the two is not known. We suggest that phosphorylation and dephosphorylation of the D1 protein, as well as the binding of the extrinsic PsbO protein to Photosystem II, play regulatory roles in directing the damaged D1 protein to the two alternative pathways.