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| Home > Publications database > SCAF1 drives the compositional diversity of mammalian respirasomes |
| Journal Article | FZJ-2025-01648 |
;
2024
Elsevier
Amsterdam
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Please use a persistent id in citations: doi:10.1016/j.bbabio.2024.149113
Abstract: The ATP synthase in themitochondria of each human being generatesabout 50 kg of ATP daily, maintaining a steady state level of about 10 g tosustain life. The enzyme has a rotarymechanism to transmit energy froma transmembrane proton motive force across the inner membrane of theorganelle (derived by respiration) to the catalytic sites where ATP isformed from ADP and phosphate. The bovine enzyme is made of 29protein subunits of 18 types, including the inhibitor protein IF1 [1,2]. Theyare organised into a rotor and a stator. The rotor consists of a membranebound c8-ring attached to a central stalk (subunits γ, δ and ε) thatprotrudes into the mitochondrialmatrix, and penetrates into the sphericalcatalytic domain (α3β3) of the stator. The stator is completed by aperipheral stalk (PS; subunits OSCP, F6, b and d), bound to the externalsurface of the catalytic domain and extending into themembrane domain(subunits ATP6 and ATP8 plus three small membrane subunits e, f and g,which form a wedge encapsulating lipid molecules). ATP6 is intimatelyassociated with the c8-ring and provides two proton half channelsinvolved in the generation of rotation. The wedges in two ATP synthasesinteract to formthe characteristic dimers that sit on the tips of the cristaeand subunit k links dimers together. The assembly of the human enzymeinvolves the formation of intermediate modules representing (i) thecatalytic domain (α3β3γδε, or F1, plus IF1), (ii) the PS plus the membrane"wedge". [3,4], and (iii) themembrane bound c8-rotor ring [5]. They formthe key intermediate F1-IF1-c8-PS [5] into which subunits ATP6 and ATP8are inserted between the c8-ring and the wedge with subunit j bound toATP6, forming the proton pathway. Two protein assembly factors arerequired to build the c8-ring and three others to assemble the catalyticdomain. IF1 is another key assembly factor that intervenes to preventpartially formed complexes that are capable of ATP hydrolysis (but notsynthesis) from doing so. The assembly pathway reflects the probablemodular path of evolution of the enzyme. Finally, I will comment on thelack of involvement of ATP synthase in the permeability transition.
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