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

FEBS Letters

Matthey, Ulrich²  Dimroth, Peter²  Henzen, Fabienne²  Meier, Thomas²  Müller, Daniel J.¹ 

[1] Max-Planck-Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany;Institut für Mikrobiologie, Eidgenössische Technische Hochschule, ETH-Zentrum, CH-8092 Zürich, Switzerland

关键词: ATP synthase;    Subunit c ring;    Phospholipid;    Atomic force microscopy;    Ilyobacter tartaricus;    AFM;    atomic force microscopy;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/S0014-5793(01)02837-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown