| Autores |
Calvo, Enrique , Cogliati, Sara , Hernansanz-Agustin, Pablo , Loureiro-Lopez, Marta , Guaras, Adela , CASUSO PÉREZ, RAFAEL, Garcia-Marques, Fernando , Acin-Perez, Rebeca , Marti-Mateos, Yolanda , Silla-Castro, J. C. , Carro-Alvarellos, Marta , Huertas, Jesus R. , Vazquez, Jesus , Enriquez, J. A. |
| Abstract |
Mitochondrial respiratory complexes assemble into supercomplexes (SC). Q-respirasome (III2 + IV) requires the supercomplex assembly factor (SCAF1) protein. The role of this factor in the N-respirasome (I + III2 + IV) and the physiological role of SCs are controversial. Here, we study C57BL/6J mice harboring nonfunctional SCAF1, the full knockout for SCAF1, or the wild-type version of the protein and found that exercise performance is SCAF1 dependent. By combining quantitative data-independent proteomics, 2D Blue native gel electrophoresis, and functional analysis of enriched respirasome fractions, we show that SCAF1 confers structural attachment between III2 and IV within the N-respirasome, increases NADH-dependent respiration, and reduces reactive oxygen species (ROS). Furthermore, the expression of AOX in cells and mice confirms that CI-CIII superassembly segments the CoQ in two pools and modulates CI-NADH oxidative capacity. |
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