Covalent modifications of histones: expression from chromatin templates.
Recent advances highlight the involvement of histone acetyltransferases in transcriptional activation and histone deacetylases in transcriptional repression. Transcription factors loaded onto regulatory DNA elements may recruit either coactivators with histone acetyltransferase activity or corepressors associated with histone deacetylases. The recruited enzymes may either acetylate or deacetylate proximal nucleosomal histones or nonhistone chromosomal proteins.
Davie
J R
JR
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Manitoba, Winnipeg, Canada. Davie@cc.umanitoba.ca
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D005786:Gene Expression Regulation; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D015530:Nuclear Matrix / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D013698:Templates, Genetic; D015533:Transcriptional Activation
D002843:Chromatin; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases