In the intact cell, DNA is closely associated with histones and other nuclear proteins to form chromatin.The remodeling of chromatin is believed to be a critical component of transcriptional regulation, and a major source of this remodeling is brought about by the acetylation of nucleosomal histones. Acetylation of lysine residues in the amino-terminal tail domain of histone results in an allosteric change in the nucleosomal conformation, and an increased accessiblity of DNA to transcription factors. Mammalian HDAC1 (also designated HD1), HDAC2 (also designated RPD3) and HDAC3, all of which are related to the yeast transcriptional regulator Rpd3p, have been identified as histone deacetylases. The retinoblastoma binding proteins RbAp46 and RbAp48 have been identified as histone binding proteins, and they are components of the histone deacetylase complex.
