Histone modifications in transcriptional regulation.
Covalent modifications of the amino termini of the core histones in nucleosomes have important roles in gene regulation. Research in the past two years reveals these modifications to consist of phosphorylation, methylation and ubiquitination, in addition to the better-characterized acetylation. This multiplicity of modifications, and their occurrence in patterns and dependent sequences, argues persuasively for the existence of a histone code.
Berger
Shelley L
SL
The Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania 19104, USA. berger@wistar.upenn.edu
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation; D051548:Histone Acetyltransferases; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D010766:Phosphorylation; D011496:Protein Methyltransferases; D011499:Protein Processing, Post-Translational; D029701:Saccharomyces cerevisiae Proteins
D002843:Chromatin; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D000123:Acetyltransferases; D051548:Histone Acetyltransferases