心磷脂与ATP合酶c亚基的相互作用：固态核磁共振表征
Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.
作者信息
Laage Ségolène, Tao Yisong, McDermott Ann E
机构信息
Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, United States.
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461, United States.
出版信息
Biochim Biophys Acta. 2015 Jan;1848(1 Pt B):260-5. doi: 10.1016/j.bbamem.2014.08.021. Epub 2014 Aug 25.
Abstract
The interaction of lipids with subunit c from F1F0 ATP synthase is studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interacts and copurifies with cardiolipin. Solid state NMR data on oligomeric rings of F0 show that the cardiolipin interacts with the c subunit in membrane bilayers. These studies offer strong support for the hypothesis that F0 has specific interactions with cardiolipin.
摘要
采用生物物理方法研究了脂质与F1F0 ATP合酶亚基c的相互作用。来自大肠杆菌和肺炎链球菌的亚基c均能与心磷脂相互作用并共同纯化。关于F0寡聚环的固态核磁共振数据表明，心磷脂在膜双层中与c亚基相互作用。这些研究为F0与心磷脂存在特异性相互作用这一假说提供了有力支持。
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