Self-assembly of ATP synthase subunit c rings

被引：49

作者：

Arechaga, I

Jonathan, P

Butler, G

Walker, JE

机构：

[1] MRC, Dunn Human Nutr Unit, Cambridge CB2 2YK, England

[2] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

FEBS LETTERS | 2002年 / 515卷 / 1-3期

关键词：

F-ATPase; subunit c; oligomerisation; analytical ultracentrifugation; electron microscopy;

D O I：

10.1016/S0014-5793(02)02447-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：189 / 193

页数：5