Rows of ATP synthase dimers in native mitochondrial inner membranes

被引:76
作者
Buzhynskyy, Nikolay
Sens, Pierre
Prima, Valerie
Sturgis, James N.
Scheuring, Simon [1 ]
机构
[1] Inst Curie, UMR168, CNRS, F-75248 Paris, France
[2] CNRS, UMR 7083, ESPCI, F-75231 Paris, France
[3] CNRS, IBSM, UPR 9027, F-13402 Marseille, France
关键词
D O I
10.1529/biophysj.107.109728
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The ATP synthase is a nanometric rotary machine that uses a transmembrane electrochemical gradient to form ATP. The structures of most components of the ATP synthase are known, and their organization has been elucidated. However, the supramolecular assembly of ATP synthases in biological membranes remains unknown. Here we show with submolecular resolution the organization of ATP synthases in the yeast mitochondrial inner membranes. The atomic force microscopy images we have obtained show how these molecules form dimers with characteristic 15 nm distance between the axes of their rotors through stereospecific interactions of the membrane embedded portions of their stators. A different interaction surface is responsible for the formation of rows of dimers. Such an organization elucidates the role of the ATP synthase in mitochondrial morphology. Some dimers have a different morphology with 10 nm stalk-to-stalk distance, in line with ATP synthases that are accessible to IF1 inhibition. Rotation torque compensation within ATP synthase dimers stabilizes the ATP synthase structure, in particular the stator-rotor interaction.
引用
收藏
页码:2870 / 2876
页数:7
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