Self-assembly of ATP synthase subunit c rings
Self-assembly of ATP synthase subunit c rings
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DOI：
10.1016/s0014-5793(02)02447-x
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发表时间：
2002-03-27
期刊：
影响因子：
3.5
通讯作者：
Walker, JE
中科院分区：
文献类型：
--
作者：
Arechaga, I;Jonathan, P;Walker, JE
H+转运ATP合酶的C亚基是其膜结构域的重要组成部分，参与跨膜质子传导。来自不同物种的亚基c的环状结构先前已被报道。然而，很少有人知道的类型的相互作用，影响形成的c-环的ATP酶复合物。在这里，我们报告的亚基c在大肠杆菌中过表达，并在非离子洗涤剂溶液中纯化自组装成环状结构的复杂的其他亚基的情况下。结果表明，亚基c的成环能力是由其一级结构决定的。(C)2002年由Elsevier Science B. V.代表欧洲生物化学学会联合会出版。
Subunit c of the H+ transporting ATP synthase is an essential part of its membrane domain that participates in transmembrane proton conduction. The annular architecture of the subunit c from different species has been previously reported. However, little is known about the type of interactions that affect the formation of c-rings in the ATPase complex. Here we report that subunit c over-expressed in Escherichia coli and purified in non-ionic detergent solutions self-assembles into annular structures in the absence of other subunits of the complex. The results suggest that the ability of subunit c to form rings is determined by its primary structure. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.