The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel
The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel
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DOI：
10.1023/a:1005621125812
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发表时间：
2000-10-01
影响因子：
3
通讯作者：
Nagley, P
中科院分区：
文献类型：
--
作者：
Devenish, RJ;Prescott, M;Nagley, P
寡霉素长期以来一直被认为是线粒体ATP合酶的抑制剂，它与F-o亚基9和6结合，这些亚基有助于复合物的质子通道功能。顾名思义，OSCP是完整酶复合物显示对寡霉素敏感性所必需的寡霉素敏感性赋予蛋白。线粒体ATP合成酶的结构和机制的最新进展导致OSCP现在被认为是外周定子柄的组成部分，而不是中央柄的组成部分。OSCP如何赋予寡霉素敏感性的酶是未知的，但可能反映了重要的蛋白质-蛋白质相互作用内组装的复合物，并向下传输定子柄，从而影响质子通道功能。我们在这里回顾我们的研究，旨在建立的化学计量，组装和功能的OSCP的知识的背景下，组织的定子柄和质子通道。
Oligomycin has long been known as an inhibitor of mitochondrial ATP synthase, putatively binding the F-o subunits 9 and 6 that contribute to proton channel function of the complex. As its name implies, OSCP is the oligomycin sensitivity-conferring protein necessary for the intact enzyme complex to display sensitivity to oligomycin. Recent advances concerning the structure and mechanism of mitochondrial ATP synthase have led to OSCP now being considered a component of the peripheral stator stalk rather than a central stalk component. How OSCP confers oligomycin sensitivity on the enzyme is unknown, but probably reflects important protein-protein interactions made within the assembled complex and transmitted down the stator stalk, thereby influencing proton channel function. We review here our studies directed toward establishing the stoichiometry, assembly, and function of OSCP in the context of knowledge of the organization of the stator stalk and the proton channel.