title: The language of covalent histone modifications.
abstract: Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a 'histone code' that is, read by other proteins to bring about distinct downstream events.
authors.affiliation: Department of Biochemistry and Molecular Genetics, University of Virginia Health Science Center, Charlottesville 22908, USA.
authors.forename: B D
authors.initials: BD
authors.lastname: Strahl
authors.forename: C D
authors.initials: CD
authors.lastname: Allis
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000502:physiology*; D006657:Histones / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008239:Lysine / Q000502:physiology; D008870:Microtubules / Q000502:physiology; D008954:Models, Biological; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D012694:Serine / Q000378:metabolism
chemical_list: D002843:Chromatin; D006657:Histones; D012694:Serine; D008239:Lysine