Fig. 3: SLC25A51 deficiency causes SIRT3 dysfunction and mitochondrial proteins hyper-acetylation.

A Western blot analysis of the acetylation levels of mitochondrial and cytoplasmic proteins of wild type and SLC25A51 knockdown LoVo (left) and HCT116 (right) cells. The relative acetylation ratio is normalized to CS and α-Tubulin respectively. B Western blot analysis of the mitochondrial proteins acetylation levels and succinylation levels of wild type and SLC25A51 knockdown HCT116 cells. The relative acetylation ratio is normalized to CS. C SLC25A51 knockdown LoVo cells were transfected with SIRT3 expressing plasmids, and the acetylation levels of mitochondrial proteins were detected by western blot. D Wild-type and SLC25A51 knockdown LoVo cells were transfected with SIRT3 expression plasmids, and the acetylation levels of SOD2 and α-Tubulin were analyzed via western blotting. E Schematic of pan-acetyllysine antibody based immunoprecipitated proteomics analysis of mitochondrial proteins extracted from wild type and SLC25A51 knockdown LoVo cells. F The silver staining of acetylated mitochondrial proteins immunoprecipitating with anti-acetyllysine agaroses in LoVo cells. G Overlapped proteins of annoted mitochondrial gene sets and acetylation elevated proteins after SLC25A51 deficiency (fold change > 1.5). H The bar graph shows the enrichment analysis of hyper-acetylated mitochondrial proteins after SLC25A51 knockdown in the terms of GO biological process. I Western blot analysis of the acetylation levels of representative proteins from the MS results in LoVo and H1299 cells.