Similarly, lack of k/Atp19 reduces dimers formation in S. It is the homolog of mammalian subunit k/DAPIT, knock-out of which reduces ATP synthesis and destabilize the dimers 9. Very little is known about the role of subunit k/Atp19. The ATP synthase monomers form dimer connected by subunits a/Atp6 interaction 7 and stabilized by the supernumerary subunits (subunits that are not essential for the catalytic activity) e/Atp21, g/Atp20 and k/Atp19 8, 9, 10. The hydrophilic F 1 domain built from the hexamer of subunits α 3 β 3 and the central stalk built from subunits γ/Atp3, δ/Atp16 and ε/Atp15, are connected to the c-ring by subunit γ 6. The matrix part of subunit b, together with subunits h/Atp14, d/Atp7, OSCP/Atp5, forms the external stalk connecting the F O with the top of the F 1. The F O domain is built from the ring of ten subunits c/Atp9, subunit a/Atp6 and the small subunits Atp8, i/Atp18, f/Atp17, and membrane part of subunit b/Atp4. It is organized into a membrane-embedded F O domain and membrane-extrinsic F 1 catalytic domain connected by two stalks: central and peripheral. cerevisiae and mammals is composed of 17 known subunits. The Saccharomyces cerevisiae as a model have provided fundamental insights into mitochondrial biology thanks to its ability to survive under fermenting conditions when OXPHOS is inactivated due to mutations in the structural and regulatory proteins of this system 5. Apart from ATP synthesis by the ATP synthase complex in the process of oxidative phosphorylation, OXPHOS 3, mitochondria is the hub for synthesis of metabolites, Fe-S clusters and essential amino acids 4. Mitochondria, the dynamic organelles of endosymbiotic origin, are the source of cellular energy in the form of ATP necessary for life and at the same time they are the origin of intrinsic signals directing the cell into programmed death pathway 1, 2. The Mco10 is an auxiliary ATP synthase subunit that only functions in permeability transition. Biochemical analysis reveal in spite of similarity in sequence and evolutionary lineage, that Mco10 and Atp19 differ significantly in function. We herein investigate the impact of Mco10 on ATP synthase functioning. In our effort to confidently define the small protein interactome of ATP synthase we found Mco10. The N-terminal part of Mco10 is very similar to k/Atp19 subunit, which along with subunits g/Atp20 and e/Atp21 plays a major role in stabilization of the ATP synthase dimers. However, recent cryo-EM structures could not ascertain Mco10 with the enzyme making questionable its role as a structural subunit. cerevisiae, the uncharacterized protein Mco10 was previously found to be associated with ATP synthase and referred as a new ‘subunit l’. The mitochondrial ATP synthase, an enzyme that synthesizes ATP and is involved in the formation of the mitochondrial mega-channel and permeability transition, is a multi-subunit complex.
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