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Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows

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Blum,  Thorsten
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hahn,  Alexander
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Meier,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Davies,  Karen M.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Blum, T., Hahn, A., Meier, T., Davies, K. M., & Kühlbrandt, W. (2019). Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows. Proceedings of the National Academy of Sciences of the United States of America, 116(10), 4250-4255. doi:10.1073/pnas.1816556116.


Cite as: https://hdl.handle.net/21.11116/0000-0003-527D-5
Abstract
Mitochondrial ATP synthases form dimers, which assemble into long ribbons at the rims of the inner membrane cristae. We reconstituted detergent-purified mitochondrial ATP synthase dimers from the green algae Polytomella sp. and the yeast Yarrowia lipolytica into liposomes and examined them by electron cryotomography. Tomographic volumes revealed that ATP synthase dimers from both species self-assemble into rows and bend the lipid bilayer locally. The dimer rows and the induced degree of membrane curvature closely resemble those in the inner membrane cristae. Monomers of mitochondrial ATP synthase reconstituted into liposomes do not bend membrane visibly and do not form rows. No specific lipids or proteins other than ATP synthase dimers are required for row formation and membrane remodelling. Long rows of ATP synthase dimers are a conserved feature of mitochondrial inner membranes. They are required for cristae formation and a main factor in mitochondrial morphogenesis.