Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity.

ABSTRACT:

Background

Sirtuins (SIRT1-7) are a family of NAD-dependent deacetylases and/or ADP-ribosyltransferases that are involved in metabolism, stress responses and longevity. SIRT3 is localized to mitochondria, where it deacetylates and activates a number of enzymes involved in fuel oxidation and energy production.

Methodology/principal findings

In this study, we performed a proteomic screen to identify SIRT3 interacting proteins and identified several subunits of complex II and V of the electron transport chain. Two subunits of complex II (also known as succinate dehydrogenase, or SDH), SDHA and SDHB, interacted specifically with SIRT3. Using mass spectrometry, we identified 13 acetylation sites on SDHA, including six novel acetylated residues. SDHA is hyperacetylated in SIRT3 KO

SUBMITTER: Finley LW 

PROVIDER: S-EPMC3157345 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature