Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs.
Reversible acetylation of lysines on the amino-terminal tails of nucleosomal histones is correlated with changes in chromatin structure and transcription. The recent characterization of enzymes directly responsible for regulating histone acetylation and deacetylation and the cloning of their encoding cDNAs have provided insights into the possible functional and regulatory mechanisms of these classes of molecules. Nuclear histone acetylases have been shown to be transcriptional coactivators and coactivator-associated proteins, while histone deacetylases have been identified as components of nuclear co-repressor complexes. These findings confirm previous studies linking histone acetylation and transcriptional regulation.
Howard Hughes Medical Institute, Harvard University Department of Chemistry, 12 Oxford Street, Cambridge, MA 02138, USA. hassig@slsiris harvard.edu.
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D000123:Acetyltransferases / Q000378:metabolism*; D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D051548:Histone Acetyltransferases; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D011485:Protein Binding; D012097:Repressor Proteins / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D014158:Transcription, Genetic
D004791:Enzyme Inhibitors; D056572:Histone Deacetylase Inhibitors; D009687:Nuclear Proteins; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases