An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases

Ondřej Gahura, Alexander Mühleip, Carolina Hierro-Yap, Brian Panicucci, Minal Jain, David Hollaus, Martina Slapničková, Alena Zíková () and Alexey Amunts ()
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Ondřej Gahura: Biology Centre, Czech Academy of Sciences
Alexander Mühleip: Stockholm University
Carolina Hierro-Yap: Biology Centre, Czech Academy of Sciences
Brian Panicucci: Biology Centre, Czech Academy of Sciences
Minal Jain: Biology Centre, Czech Academy of Sciences
David Hollaus: University of South Bohemia
Martina Slapničková: Biology Centre, Czech Academy of Sciences
Alena Zíková: Biology Centre, Czech Academy of Sciences
Alexey Amunts: Stockholm University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-33588-z

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