TY  - JOUR
A1  - Blum, Thorsten
A1  - Hahn, Alexander
A1  - Meier, Thomas
A1  - Davies, Karen M.
A1  - Kühlbrandt, Werner
T1  - Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows
T2  - Proceedings of the National Academy of Sciences of the United States of America
N2  - 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.
KW  - mitochondria
KW  - ATP synthase
KW  - membrane curvature
KW  - electron cryotomography
KW  - subtomogram averaging
Y1  - 2019
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/49141
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-491414
SN  - 1091-6490
SN  - 0027-8424
N1  - Copyright © 2019 the Author(s). Published by PNAS.
This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
VL  - 116
IS  - Art. 201816556
SP  - 1
EP  - 6
PB  - National Acad. of Sciences
CY  - Washington, DC
ER  -