Cardiolipin Affects the Supramolecular Organization of ATP Synthase in Mitochondria

被引:196
|
作者
Acehan, Devrim [1 ,2 ]
Malhotra, Ashim [3 ]
Xu, Yang [3 ]
Ren, Mindong [1 ]
Stokes, David L. [1 ,2 ,4 ]
Schlame, Michael [1 ,3 ]
机构
[1] NYU, Sch Med, Dept Cell Biol, New York, NY 10016 USA
[2] NYU, Sch Med, Struct Biol Program, Skirball Inst, New York, NY USA
[3] NYU, Sch Med, Dept Anesthesiol, New York, NY 10016 USA
[4] New York Struct Biol Ctr, New York, NY USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
BEEF-HEART MITOCHONDRIA; ADP/ATP CARRIER PROTEIN; CRYOELECTRON TOMOGRAPHY; RESPIRATORY-CHAIN; INNER MEMBRANES; BARTH-SYNDROME; MUTANT; DYSFUNCTION; CRISTAE; DIMER;
D O I
10.1016/j.bpj.2011.03.031
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
F1F0 ATP synthase forms dimers that tend to assemble into large supramolecular structures. We show that the presence of cardiolipin is critical for the degree of oligomerization and the degree of order in these ATP synthase assemblies. This conclusion was drawn from the statistical analysis of cryoelectron tomograms of cristae vesicles isolated from Drosophila flight-muscle mitochondria, which are very rich in ATP synthase. Our study included a wild-type control, a cardiolipin synthase mutant with nearly complete loss of cardiolipin, and a tafazzin mutant with reduced cardiolipin levels. In the wild-type, the high-curvature edge of crista vesicles was densely populated with ATP synthase molecules that were typically organized in one or two rows of dimers. In both mutants, the density of ATP synthase was reduced at the high-curvature zone despite unchanged expression levels. Compared to the wild-type, dimer rows were less extended in the mutants and there was more scatter in the orientation of dimers. These data suggest that cardiolipin promotes the ribbonlike assembly of ATP synthase dimers and thus affects lateral organization and morphology of the crista membrane.
引用
收藏
页码:2184 / 2192
页数:9
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