Single particle analysis of thylakoid proteins from Thermosynechococcus elongatus and Synechocystis 6803:: Localization of the CupA subunit of NDH-1
Single particle analysis of thylakoid proteins from Thermosynechococcus elongatus and Synechocystis 6803:: Localization of the CupA subunit of NDH-1
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DOI：
10.1016/j.febslet.2007.12.012
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发表时间：
2008-01-01
期刊：
影响因子：
3.5
通讯作者：
Boekema, Egbert J.
中科院分区：
文献类型：
--
作者：
Folea, I. Mihaela;Zhang, Pengpeng;Boekema, Egbert J.
较大的蛋白质复合物的蓝藻光合膜的Thermosynecrocuselongatus和集胞藻6803进行了研究，通过单粒子电子显微镜洗涤剂溶解后，没有任何纯化步骤。除了与复合体1相关的“标准”L形NDH-1 L复合体之外，在两种蓝藻中发现了大量的U形NDH-1 MS复合体。在集胞藻Delta cupA和Delta cupAlcupB突变体的膜中，U形复合物不存在，这表明CupA通过结合在NDH-1 MS的膜结合臂的尖端来形成U形。比较在CO2或3 '/0 CO2空气水平下生长的膜表明，在低CO2下，NDH-1 MS颗粒的数量高出30倍。(C)2007年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The larger protein complexes of the cyanobacterial photosynthetic membrane of Thermosynechoccus elongatus and Synechocystis 6803 were studied by single particle electron microscopy after detergent solubilization, without any purification steps. Besides the "standard" L-shaped NDH-1L complex, related to complex 1, large numbers of a U-shaped NDH-1MS complex were found in both cyanobacteria. In membranes from Synechocystis Delta cupA and Delta cupAlcupB mutants the U-shaped complexes were absent, indicating that CupA is responsible for the U-shape by binding at the tip of the membrane-bound arm of NDH-1MS. Comparison of membranes grown under air levels Of CO2 or 3'/0 CO2 indicates that the number of NDH-1MS particles is 30-fold higher under low-CO2. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.