SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient- and exercise-induced stress.

作者: Athanassios Vassilopoulos , J. Daniel Pennington , Thorkell Andresson , David M. Rees , Allen D. Bosley

DOI: 10.1089/ARS.2013.5420

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摘要: Abstract Aims: Adenosine triphosphate (ATP) synthase uses chemiosmotic energy across the inner mitochondrial membrane to convert adenosine diphosphate and orthophosphate into ATP, whereas genetic deletion of Sirt3 decreases ATP levels. Here, we investigate mechanistic connection between SIRT3 homeostasis. Results: By using both in vitro vivo experiments, demonstrate that F1 proteins alpha, beta, gamma, Oligomycin sensitivity-conferring protein (OSCP) contain SIRT3-specific reversible acetyl-lysines are evolutionarily conserved bind SIRT3. OSCP was further investigated lysine 139 is a nutrient-sensitive SIRT3-dependent deacetylation target. Site directed mutants OSCPK139 directs, at least part, production mice lacking exhibit decreased muscle levels, increased acetylation, an exercise-induced stress-deficient phenotype. Innovation: This work connects aging...

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