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

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 electr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2019-03, Vol.116 (10), p.4250-4255
Main Authors: Blum, Thorsten B., Hahn, Alexander, Meier, Thomas, Davies, Karen M., Kühlbrandt, Werner
Format: Article
Language:English
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1816556116