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

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America

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.

Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1559185
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Vol. 116, Issue 10; ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)Copyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 140 works
Citation information provided by
Web of Science

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Cited By (19)

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A mitochondrial megachannel resides in monomeric F1FO ATP synthase journal December 2019
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Live-cell STED nanoscopy of mitochondrial cristae journal August 2019
Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes journal January 2020
Single organelle function and organization as estimated from Arabidopsis mitochondrial proteomics journal November 2019
Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1 journal June 2019
Response to Comment on “Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry” journal November 2019
Functional Interplay between Cristae Biogenesis, Mitochondrial Dynamics and Mitochondrial DNA Integrity journal September 2019
The Phyre2 web portal for protein modeling, prediction and analysis journal May 2015
Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes. text January 2020
Single organelle function and organization as estimated from Arabidopsis mitochondrial proteomics other January 2020
The Unique Cysteine of F-ATP Synthase OSCP Subunit Participates in Modulation of the Permeability Transition Pore journal September 2020
Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore journal September 2019
Rcf2 revealed in cryo-EM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes journal April 2020
Consequences of Folding the Mitochondrial Inner Membrane journal June 2020
Functional Interplay between Cristae Biogenesis, Mitochondrial Dynamics and Mitochondrial DNA Integrity journal September 2019
VDAC—A Primal Perspective journal February 2021
ATP synthase: evolution, energetics, and membrane interactions text January 2020