期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2003
卷号：100
期号：23
页码：13235-13240
DOI：10.1073/pnas.2135169100
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The mitochondrial ATP synthase is made of a membrane-integrated F0 component that forms a proton-permeable pore through the inner membrane and a globular peripheral F1 domain where ATP is synthesized. The catalytic mechanism is thought to involve the rotation of a 10-12 c subunit ring in the F0 together with the {gamma} subunit of F1. An important and not yet resolved question is to define precisely how the {gamma} subunit is connected with the c-ring. In this study, using a doxycycline-regulatable expression system, we provide direct evidence that the rest of the enzyme can assemble without the {delta} subunit of F1, and we show that {delta}-less mitochondria are uncoupled because of an F0-mediated proton leak. Based on these observations, and taking into account high-resolution structural models, we propose that subunit {delta} plays a key role in the mechanical coupling of the c-ring to subunit {gamma}.
