Acetylation of the e-amino group of specific lysine residues of core histones – principally but not exclusively in their unstructured N-terminal tails – is a key biochemical modification for establishing the transcriptional competence of genes bound by such histones. High resolution mapping of acetylated core histones by chromatin IPs (ChIPs) has shown them to be preferentially located at the promoters and enhancers of active genes rather than throughout the transcribed regions. Particular distributions of acetylated lysines are part of the nucleosomal ‘histone code’ that defines and to a considerable extent determines the functional status of the local chromatin. HHe istone acetylation is deposited and removed by numerous histone acetyltransferases (HATs) and deacetylases (HDACs) and acetyl-lysines are recognised (i.e. the histone code is ‘read’) by bromodomain-containing proteins.
Multiple Histone Acetyltransferases Are Associated with a Chicken Erythrocyte Chromatin Fraction Enriched in Active Genes