The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as ``readers'' of histone acetylation marks regulating the transcription of target promoters. p300/CBP-associated factor (PCAF) is a transcriptional coactivator that works both as a histone lysine acetyltransferase, through its HAT domai