The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids

被引：70
作者：
Meier, T
Matthey, U
Henzen, F
Dimroth, P [1 ]
Müller, DJ
机构：
[1] Swiss Fed Inst Technol, Inst Mikrobiol, ETH Zentrum, CH-8092 Zurich, Switzerland
[2] Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany
来源：
FEBS LETTERS | 2001年 / 505卷 / 03期
关键词：
ATP synthase; subunit c ring; phospholipid; atomic force microscopy; Hyobacter tartaricus;
D O I：
10.1016/S0014-5793(01)02837-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：
The isolated rotor cylinder of the ATP synthase from Ilyobacter tartaricus was reconstituted into two-dimensional crystalline arrays. Atomic force microscopy imaging indicated a central cavity on one side of the rotor and a central plug protruding from the other side. Upon incubation with phospholipase C, the plug disappeared, but the appearance of the surrounding c subunit oligomer was not affected. This indicates that the plug consists of phospholipids. As the detergent-purified c cylinder is completely devoid of phospholipids, these are incorporated into the central hole from one side of the cylinder during the reconstitution procedure. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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页码：353 / 356
页数：4
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