title: Dynamic fuzziness during linker histone action.
abstract: Linker histones are multi-domain nucleosome binding proteins that stabilize higher order chromatin structures and engage in specific protein-protein interactions. Here we emphasize the structural and functional properties of the linker histone C-terminal domain (CTD), focusing on its intrinsic disorder, interaction-induced secondary structure formation and dynamic fuzziness. We argue that the fuzziness inherent in the CTD is a primary molecular mechanism underlying linker histone function in the nucleus.
authors.affiliation: Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado, USA.
authors.forename: Steven J
authors.initials: SJ
authors.lastname: McBryant
authors.forename: Jeffrey C
authors.initials: JC
authors.lastname: Hansen
mesh_terms: D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D009707:Nucleosomes; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D011506:Proteins