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Updated: Feb 18, 2026
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
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Non-bilayer structures in mitochondrial membranes regulate ATP synthase activity.
Sardar E Gasanov1, Aleksandr A Kim2, Lev S Yaguzhinsky3
1Applied Mathematics and Informatics Department, M.V. Lomonosov Moscow State University Branch, 22-a Amir Timur Avenue, Tashkent 100061, Uzbekistan; Bioenergetics Department, A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Vorobievy Gory, Moscow 119991, Russia.
Biochimica Et Biophysica Acta. Biomembranes
|November 29, 2017
Summary
Cardiolipin (CL) and ATP synthase promote non-bilayer structures in mitochondria to boost ATP synthesis. This study reveals how CL binding to ATP synthase enhances proton flow and energy production.
Area of Science:
- Mitochondrial biology
- Biophysics
- Biochemistry
Background:
- Cardiolipin (CL) is crucial for inner mitochondrial membrane (IMM) integrity and function.
- CL's role in forming non-bilayer structures and its precise mechanism in ATP synthesis are not fully understood.
Purpose of the Study:
- To investigate the biophysical mechanisms by which CL and ATP synthase generate non-bilayer structures.
- To determine how these structures contribute to enhanced ATP synthesis.
Main Methods:
- Proton Nuclear Magnetic Resonance (¹H NMR) and Phosphorus-31 Nuclear Magnetic Resonance (³¹P NMR) spectroscopy.
- Incubation of intact mitochondria and model membranes with toxins (CTII) and proteins (DCCD-BPF).
- Native Polyacrylamide Gel Electrophoresis (Native PAGE) and molecular docking studies.
Main Results:
- Elevated temperatures, lower pH, and CTII toxin increased non-bilayer structure formation, stimulating ATP synthesis.
- The F₀ sector of ATP synthase, specifically the DCCD-binding protein (DCCD-BPF), facilitated non-bilayer structures.
- CL uniquely bound to DCCD-BPF, forming stable lipid-protein complexes, with two identified CL binding sites.
Conclusions:
- CL and ATP synthase cooperate to form non-bilayer structures at the IMM.
- These structures facilitate proton clustering and ATP synthase complex aggregation, enhancing proton translocation and ATP synthesis.
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