ABSTRACT
Although many of the functions of the genome are influenced by the methylation state of DNA, the importance of histone modification for gene expression control cannot be understated. By recognizing regions of acetylated histones and by recruiting other proteins capable of remodeling chromatin conformation, bromodomain-containing proteins are able to reinforce the open conformation of chromatin where higher levels of histone acetylation are present. Sequence-specific lysine acetylation recognition by a bromodomain is dependent on how the bromodomain recognizes target protein residues flanking the acetyl-lysine, and that, in turn, will most probably depend on other structural elements in the transcription factor or other bromodomain protein. Analyses of other genes that show evidence of H3S10 phosphorylation similarly suggest that the presence of a phosphorylated H3 terminal tail does not necessarily predispose that tail to acetylation at lysine 14, meaning that other factors are necessary to induce activation of the locus.
