title: Functional consequences of histone modifications.
abstract: Covalent modifications of the histone proteins have well-known roles in gene expression. Experiments reported during the past year have extended this paradigm to include roles for histone acetylation and phosphorylation in DNA double-strand break repair. In addition, new results now provide a definitive example of an acetylation histone code, whereas others reveal the workings of a charge patch mechanism. Finally, exciting research has identified new modifications, complex modification cascades, and functional links to DNA methylation and RNA interference pathways.
authors.affiliation: Department of Microbiology, University of Virginia, 1300 Jefferson Park Avenue, Charlottesville, Virginia 22908, USA.
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Iizuka
authors.forename: M Mitchell
authors.initials: MM
authors.lastname: Smith
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000502:physiology; D000818:Animals; D006657:Histones / Q000502:physiology*; D006801:Humans; D008745:Methylation; D008780:Methyltransferases / Q000502:physiology; D010766:Phosphorylation; D010770:Phosphotransferases / Q000502:physiology; D012313:RNA / Q000502:physiology; D012568:Schizosaccharomyces / Q000502:physiology
chemical_list: D006657:Histones; D012313:RNA; D008780:Methyltransferases; D000123:Acetyltransferases; D010770:Phosphotransferases