InterPro domain: IPR037138

Regulation of transcription is, in part, modulated by reversible histone acetylation on several lysine. Histone deacetylases (HDA) catalyse the removalof the acetyl group. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of this ancient protein superfamily [ 1 ].

HDAs function in multi-subunit complexes, reversing the acetylation of histones by histone acetyltransferases [ 2 , 3 ], and are also believed to deacetylate general transcription factors such as TFIIF and sequence-specific transcription factors such as p53 [ 4 ]. Thus, HDAs contribute to the regulation of transcription, in particular transcriptional repression [ 4 ]. At N-terminal tails of histones, removal of the acetyl group from the epsilon-amino group of a lysine side chain will restore its positivecharge, which may stabilise the histone-DNA interaction and prevent activating transcription factors binding to promoter elements [ 4 ]. HDAs play important roles in the cell cycle and differentiation, and their deregulation can contribute to the development of cancer [ 4 , 4 ].

This entry represents the structural domain superfamily found in histone deacetylases. It consists of a 3-layer(alpha-beta-alpha) sandwich.

1. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res. 25, 3693-7
2. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9, 193-8
3. Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9, 40-8
4. Histone acetylation and cancer. Curr. Opin. Genet. Dev. 9, 171-4