title: Nucleosome sliding mechanisms: new twists in a looped history.
abstract: Nucleosomes, the basic organizational units of chromatin, package and regulate eukaryotic genomes. ATP-dependent nucleosome-remodeling factors endow chromatin with structural flexibility by promoting assembly or disruption of nucleosomes and the exchange of histone variants. Furthermore, most remodeling factors induce nucleosome movements through sliding of histone octamers on DNA. We summarize recent progress toward unraveling the basic nucleosome sliding mechanism and the interplay of the remodelers' DNA translocases with accessory domains. Such domains optimize and regulate the basic sliding reaction and exploit sliding to achieve diverse structural effects, such as nucleosome positioning or eviction, or the regular spacing of nucleosomes in chromatin.
authors.affiliation: 1] Adolf-Butenandt-Institute, Ludwig-Maximilians-Universität, Munich, Germany. [2] Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität, Munich, Germany.
authors.forename: Felix
authors.initials: F
authors.lastname: Mueller-Planitz
authors.forename: Henrike
authors.initials: H
authors.lastname: Klinker
authors.forename: Peter B
authors.initials: PB
authors.lastname: Becker
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D020029:Base Pairing; D042002:Chromatin Assembly and Disassembly; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D042003:DNA Packaging; D006657:Histones / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism
chemical_list: D006657:Histones; D009707:Nucleosomes; D014157:Transcription Factors; D004247:DNA; D000251:Adenosine Triphosphatases