Litcius/Paper detail

TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I

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

2021Proceedings of the National Academy of Sciences48 citationsDOIOpen Access PDF

Abstract

-ring, which provides the membrane sector of the enzyme's rotor, and its assembly is influenced by another transmembrane (TMEM) protein, TMEM70. We have shown that subunit c interacts with TMEM70 and another hitherto unidentified mitochondrial transmembrane protein, TMEM242. Deletion of TMEM242, similar to deletion of TMEM70, affects but does not completely eliminate the assembly of ATP synthase, and to a lesser degree the assembly of respiratory enzyme complexes I, III, and IV. Deletion of TMEM70 and TMEM242 together prevents assembly of ATP synthase and the impact on complex I is enhanced. Removal of TMEM242, but not of TMEM70, also affects the introduction of subunits ATP6, ATP8, j, and k into the enzyme. TMEM70 and TMEM242 interact with the mitochondrial complex I assembly (the MCIA) complex that supports assembly of the membrane arm of complex I. The interactions of TMEM70 and TMEM242 with MCIA could be part of either the assembly of ATP synthase and complex I or the regulation of their levels.

Topics & Concepts

ATP synthaseChemiosmosisMembraneRotor (electric)F-ATPaseInner membraneMitochondrionRing (chemistry)BiophysicsDomain (mathematical analysis)ATP synthase gamma subunitProtonChemistryATPaseBiochemistryBiologyATP hydrolysisEnzymePhysicsGeneOrganic chemistryChloroplastThylakoidQuantum mechanicsMathematical analysisMathematicsATP Synthase and ATPases ResearchMitochondrial Function and PathologyPhotosynthetic Processes and Mechanisms