title: Structures and interactions of the core histone tail domains.
abstract: The core histone tail domains are "master control switches" that help define the structural and functional characteristics of chromatin at many levels. The tails modulate DNA accessibility within the nucleosome, are essential for stable folding of oligonucleosome arrays into condensed chromatin fibers, and are important for fiber-fiber interactions involved in higher order structures. Many nuclear signaling pathways impinge upon the tail domains, resulting in posttranslational modifications that are likely to alter the charge, structure, and/or interactions of the core histone tails or to serve as targets for the binding of ancillary proteins or other enzymatic functions. However, currently we have only a marginal understanding of the molecular details of core histone tail conformations and contacts. Here we review data related to the structures and interactions of the core histone tail domains and how these domains and posttranslational modifications therein may define the structure and function of chromatin.
authors.affiliation: Department of Biochemistry and Biophysics, University of Rochester Medical Center, NY 14642, USA.
authors.forename: Chunyang
authors.initials: C
authors.lastname: Zheng
authors.forename: Jeffrey J
authors.initials: JJ
authors.lastname: Hayes
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002843:Chromatin / Q000737:chemistry / Q000235:genetics / Q000648:ultrastructure; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D002843:Chromatin; D006657:Histones; D004247:DNA