Identification of complex V subunits with the Lys residues that are acetylated in dcerk1 and dsirt2 mutants. (A) GO analysis (biological process component) of the Drosophila mitochondrial acetylome shows significant enrichment of OXPHOS complexes, particularly, complex I and complex V. The numbers indicate the number of acetylated subunits out of the total number of OXPHOS subunits in each complex. (B) Distribution of acetyl-Lys sites identified in each acetylated protein of the OXPHOS complexes shows 70% of the proteins have more than one site of acetylation. (C) GO analysis (biological process component) of the acetylated proteins that increase in dsirt2 features OXPHOS complex I and complex V prominently. The numbers indicate the number of acetylated subunits out of the total number of OXPHOS subunits in each complex in the dsirt2 mutant. (D) Mass spectrometric identification of the Lys residues that are acetylated in dcerk1 and dsirt2 (1.5-fold or more) in different subunits of complex V. For Lys residues that are conserved, the corresponding human Lys is shown. Asterisks denote Lys residues that have been identified as acetylated in other proteomic surveys. The blue numbers indicate modified Lys residues identified both in dcerk1 and dsirt2 mutants.
