Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase beta and regulates complex V activity
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Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase beta and regulates complex V activity" (2014). Comments This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity.
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Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity
Adenosine triphosphate (ATP) synthase β, the catalytic subunit of mitochondrial complex V, synthesizes ATP. We show that ATP synthase β is deacetylated by a human nicotinamide adenine dinucleotide (NAD(+))-dependent protein deacetylase, sirtuin 3, and its Drosophila melanogaster homologue, dSirt2. dsirt2 mutant flies displayed increased acetylation of specific Lys residues in ATP synthase β and...
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