| Autor: |
Bahri, Hela, Buratto, Jérémie, Rojo, Manuel, Dompierre, Jim, Salin, Bénédicte, Blancard, Corinne, Cuvellier, Sylvain, Rose, Marie, Ammar Elgaaied, Amel Ben, Tetaud, Emmanuel, di Rago, Jean-Paul, Devin, Anne, Duvezin-Caubet, Stéphane |
| Jazyk: |
angličtina |
| Rok vydání: |
2020 |
| DOI: |
10.1101/2020.04.03.023861 |
| Popis: |
Mitochondrial ATP-synthesis is catalyzed by F1Fo-ATP synthase, an enzyme of dual genetic origin. TMEM70, a transmembrane protein mutated in neonatal encephalo-cardiomyopathies, is required for assembly/stability of ATP-synthase, but its precise role remains largely unknown. Herein, we demonstrate a role of TMEM70 in the formation of the c-ring (an oligomer of 8 c-subunits/Su.c) essential for Fo-mediated proton transport. Immunoprecipitation and two-dimensional blue-native/SDS-PAGE reveal interactions between TMEM70 and Su.c not yet assembled into the ATP synthase, and provide evidence for oligomerization of TMEM70 into homo-oligomers of 8 TMEM70 dimers. Analysis of ATP-synthase assembly in cells devoid of TMEM70, mitochondrial DNA or F1 subunits indicate that TMEM70 oligomers provide a scaffold for c-ring assembly, regardless of the presence of other ATP synthase subunits or of mitochondrial bioenergetics status. Expansion super-resolution microscopy depicting mitochondrial ultrastructure reveals the specific localization of TMEM70 within inner membrane cristae. This indicates that ATP synthase, localizing to the edge of cristae, is assembled within inner cristae membranes rather than at the inner boundary membrane that is apposed to the outer membrane. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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