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

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Title: Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows
Authors: Blum, TB
Hahn, A
Meier, T
Davies, KM
Kuhlbrandt, W
Item Type: Journal Article
Abstract: Mitochondrial ATP synthases form dimers, which assemble intolong ribbons at the rims of the inner membrane cristae. We re-constituted detergent-purified mitochondrial ATP synthase dimersfrom the green algaPolytomellasp. and the yeastYarrowialipolyticainto liposomes and examined them by electron cryo-tomography. Tomographic volumes revealed that ATP synthasedimers from both species self-assemble into rows and bend thelipid bilayer locally. The dimer rows and the induced degree ofmembrane curvature closely resemble those in the inner mem-brane cristae. Monomers of mitochondrial ATP synthase reconsti-tuted into liposomes do not bend membrane visibly and do notform rows. No specific lipids or proteins other than ATP synthasedimers are required for row formation and membrane remodelling.Long rows of ATP synthase dimers are a conserved feature ofmitochondrial inner membranes. They are required for cristaeformation and a main factor in mitochondrial morphogenesis.
Issue Date: 13-Feb-2019
Date of Acceptance: 3-Jan-2019
URI: http://hdl.handle.net/10044/1/66345
ISSN: 0027-8424
Publisher: National Academy of Sciences
Journal / Book Title: Proceedings of the National Academy of Sciences of the United States of America
Keywords: MD Multidisciplinary
Publication Status: Accepted
Embargo Date: publication subject to indefinite embargo
Appears in Collections:Faculty of Natural Sciences

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