In the intact cell, DNA closely associates 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 accessibility to transcription factors by DNA. Conversely, the deacetylation of histones is associated with transcriptional silencing. Several mammalian proteins have been identified as nuclear histone acetylases, including GCN5, PCAF (p300/CBPassociated factor), p300/CBP, HAT1, and the TFIID subunit TAF II p250. Mammalian HDAC1 (also designated HD1), HDAC2 (also designated RPD3) and HDAC3-6, have been identified as histone deacetylases.This enzyme deacetylates lysine residues in histones H2A, H2B, H3 and H4.