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Functional role of respiratory supercomplexes in mice: SCAF1 relevance and segmentation of the Qpool.

Science advances (2020-07-09)
Enrique Calvo, Sara Cogliati, Pablo Hernansanz-Agustín, Marta Loureiro-López, Adela Guarás, Rafael A Casuso, Fernando García-Marqués, Rebeca Acín-Pérez, Yolanda Martí-Mateos, J C Silla-Castro, Marta Carro-Alvarellos, Jesús R Huertas, Jesús Vázquez, J A Enríquez
RESUMEN

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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Millipore
Membrana de PVDF Immobilon®-FL, 1 roll, 27 cm x 3.75 m, 0.45 µm pore size, Hydrophobic PVDF Transfer Membrane with low background fluorescence for Western blotting. Compatible with visible and infrared fluorescent probes.
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Digitonina, ~50% (TLC)
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