Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions.

Data from ProteomeXchange, PXD ID: PXD000885. File: 20110706_VELOS1_BTW_SA_C2T1_F02.mzml. Published as part of . From the Abstract: {{i}} Acetylation is frequently detected on mitochondrial enzymes, and the sirtuin deacetylase SIRT3 is thought to regulate metabolism by deacetylating mitochondrial proteins. However, the stoichiometry of acetylation has not been studied and is important for understanding whether SIRT3 regulates or suppresses acetylation. Using quantitative mass spectrometry, we measured acetylation stoichiometry in mouse liver tissue and found that SIRT3 suppressed acetylation to a very low stoichiometry at its target sites. By examining acetylation changes in the liver, heart, brain, and brown adipose tissue of fasted mice, we found that SIRT3-targeted sites were mostly unaffected by fasting, a dietary manipulation that is thought to regulate metabolism through SIRT3-dependent deacetylation. {{/i}}