title: Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure.
abstract: Eukaryotic chromatin is a hierarchical collection of nucleoprotein structures that package DNA to form chromosomes. The initial levels of packaging include folding of long strings of nucleosomes into secondary structures and array-array association into higher-order tertiary chromatin structures. The core histone tail domains are required for the assembly of higher-order structures and mediate short- and long-range intra- and inter-nucleosome interactions with both DNA and protein targets to direct their assembly. However, important details of these interactions remain unclear and are a subject of much interest and recent investigations. Here, we review work defining the interactions of the histone N-terminal tails with DNA and protein targets relevant to chromatin higher-order structures, with a specific emphasis on the contributions of H3 and H4 tails to oligonucleosome folding and stabilization. We evaluate both classic and recent experiments determining tail structures, effect of tail cleavage/loss, and posttranslational modifications of the tails on nucleosomes and nucleosome arrays, as well as inter-nucleosomal and inter-array interactions of the H3 and H4 N-terminal tails.
authors.affiliation: Department of Biochemistry and Biophysics, University of Rochester Medical Center, University of Rochester, 601 Elmwood Ave, Box 712, Rochester, NY, 14625, USA.
authors.forename: Sharon
authors.initials: S
authors.lastname: Pepenella
authors.forename: Kevin J
authors.initials: KJ
authors.lastname: Murphy
authors.forename: Jeffrey J
authors.initials: JJ
authors.lastname: Hayes
mesh_terms: D000107:Acetylation; D000818:Animals; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D006657:Histones; D009707:Nucleosomes