An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases

0563704 - BC 2023 RIV GB eng J - Článek v odborném periodiku
Gahura, Ondřej - Muhleip, A. - Hierro Yap, Carolina - Panicucci, Brian - Jain, Minal - Hollaus, D. - Slapničková, Martina - Zíková, Alena - Amunts, A.
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.
Nature Communications. Roč. 13, č. 1 (2022), č. článku 5989. E-ISSN 2041-1723
Grant CEP: GA ČR(CZ) GA18-17529S; GA ČR(CZ) GJ20-04150Y; GA MŠMT(CZ) EF16_019/0000759
Institucionální podpora: RVO:60077344
Klíčová slova: Mitochondrial * synthase * lineage
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 16.6, rok: 2022
Způsob publikování: Open access
https://www.nature.com/articles/s41467-022-33588-z

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.
Trvalý link: https://hdl.handle.net/11104/0339020