Litcius/Paper detail

Assembly of the peripheral stalk of ATP synthase in human mitochondria

Jiuya He, Joe Carroll, Shujing Ding, Ian M. Fearnley, M.G. Montgomery, John E. Walker

2020Proceedings of the National Academy of Sciences44 citationsDOIOpen Access PDF

Abstract

Significance The production of ATP in mitochondria requires the oxidation of energy rich compounds to generate a proton motive force (pmf), a chemical potential difference for protons across the inner membrane. This pmf powers the ATP synthase, a molecular machine with a rotary action, to synthesize ATP. The assembly of human ATP synthase from 27 nuclear encoded proteins and two mitochondrially encoded subunits in the inner organellar membrane involves the formation of intermediate modules representing the F 1 -catalytic domain, the peripheral stalk, associated membrane subunits, and the c 8 ring in the membrane part of the rotor. Here, we describe how components of the peripheral stalk and three associated membrane subunits are assembled and introduced into the enzyme complex.

Topics & Concepts

ATP synthaseStalkATP synthase gamma subunitChemiosmosisMitochondrionInner membraneMembraneV-ATPaseInner mitochondrial membraneATP–ADP translocaseBiophysicsBiochemistryATP hydrolysisEnzymeF-ATPaseChemistryATPaseBiologyGeneChloroplastThylakoidHorticultureATP Synthase and ATPases ResearchMitochondrial Function and PathologyPhotosynthetic Processes and Mechanisms