Reference: Buzhynskyy N, et al. (2007) Rows of ATP synthase dimers in native mitochondrial inner membranes. Biophys J 93(8):2870-6

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Abstract


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 organisation has been elucidated. However, the supramolecular assembly of ATP synthases in biological membranes remains unknown. Here we show with sub-molecular resolution the organisation of ATP synthases in the yeast mitochondrial inner membranes (MIM). The atomic force microscopy (AFM) images we have obtained show how these molecules form dimers with characteristic 15nm distance between the axes of their rotors through stereo-specific interactions of the membrane embedded portions of their stators. A different interaction surface is responsible for the formation of rows of dimers. Such an organisation elucidates the role of the ATP-synthase in mitochondrial morphology. Some dimers have a different morphology with 10nm 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.

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Journal Article
Authors
Buzhynskyy N, Sens P, Prima V, Sturgis JN, Scheuring S
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