ArticleNature communications2022
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 25 citations in OpenAlex.
- Trypanosomal MICOS Is Assembled on Non-Respiring Mitochondrial Crista Precursors and Associates With Two Integral Microproteins.Molecular microbiology · 2026Article
- Article
- Conserved and divergent mitochondrial assemblies in kinetoplastid parasites.Molecular cell · 2026Article
- The molecular mechanisms of crista formation: how mitochondria give themselves breathing room.Biochemical Society transactions · 2026Review
- Proteolytic processing of the unique FScientific reports · 2026Article
- Reversal of ATP synthase is a key attribute accompanying cellular differentiation of Trypanosoma brucei insect forms.Communications biology · 2026Article
- Genetic origins and proteomic consequences of kinetoplast loss in trypanosomes.PLoS pathogens · 2026Article
- Unconventional model organisms bend our view on mitochondrial cristae.Journal of cell science · 2026Review
- Cryo-EM structure of the brine shrimp mitochondrial ATP synthase suggests an inactivation mechanism for the ATP synthase leak channel.Cell death and differentiation · 2025Article
- Evolutionary divergent kinetoplast genome structure and RNA editing patterns in the trypanosomatidProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Euglena's atypical respiratory chain adapts to the discoidal cristae and flexible metabolism.Nature communications · 2024Article
- The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography.The Biochemical journal · 2024Article
- Lessons from the deep: mechanisms behind diversification of eukaryotic protein complexes.Biological reviews of the Cambridge Philosophical Society · 2023Article
- Functional and biochemical characterization of the Toxoplasma gondii succinate dehydrogenase complex.PLoS pathogens · 2023Article
- Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions.Cell death and differentiation · 2023Review
- The Ancestral Shape of the Access Proton Path of Mitochondrial ATP Synthases Revealed by a Split Subunit-a.Molecular biology and evolution · 2023Article
- The persistent homology of mitochondrial ATP synthases.iScience · 2023Article
- The mystery of massive mitochondrial complexes: the apicomplexan respiratory chain.Trends in parasitology · 2022Review
- Algal photosystem I dimer and high-resolution model of PSI-plastocyanin complex.Nature plants · 2022Article
- Structures ofScience (New York, N.Y.) · 2022Article
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. The model consists of 25 subunits, including nine lineage-specific, as well as 36 lipids. The rotary mechanism is influenced by the divergent peripheral stalk, conferring a greater conformational flexibility. Proton transfer in the lumenal half-channel occurs via a chain of five ordered water molecules. The dimerization interface is formed by subunit-g that is critical for interactions but not for the catalytic activity. Although overall dimer architecture varies among eukaryotes, we find that subunit-g together with subunit-e form an ancestral oligomerization motif, which is shared between the trypanosomal and mammalian lineages. Therefore, our data defines the subunit-g/e module as a structural component determining ATP synthase oligomeric assemblies.
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