Alteration of gene expression in differentiating C2C12 cells upon inhibition of PCAF by embelin

KAT2B (PCAF) belongs to GNAT family of lysine acetyltransferases (KAT), which specifically acetylates histone H3K9 residue and several nonhistone proteins. PCAF is also a transcription coactivator. Due to the lack of PCAF, KAT specific small molecule inhibitor, the exclusive role of the acetyltransferase activity of PCAF is not well understood. Here we report that a hydroxy benzoquinone class of natural compound, embelin, specifically inhibits H3Lys9 acetylation in mice and recombinant PCAF mediated acetylation with near complete specificity in vitro. Further, using embelin, we have identified the PCAF regulated gene networks during muscle differentiation, further highlighting the broader regulatory functions of PCAF in muscle differentiation, apart from regulation through MyoD acetylation. C2C12 cells were treated with either DMSO or 10uM embelin in GM/DM for either 24 or 48h.