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 accessibility of DNA to transcription factors. Conversely, the deacetylation of histones is associated with transcriptional silencing.