title: Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1.
abstract: The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of the histone H3-H4 complex with the human retinoblastoma-associated protein RbAp48 and their exchange with a second histone chaperone, anti-silencing function protein 1 (ASF1). Exchange of histones H3-H4 between these two histone chaperones has a central role in the assembly of new nucleosomes, and we show here that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, UK.
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Marek
authors.initials: M
authors.lastname: Tyl
authors.forename: Richard
authors.initials: R
authors.lastname: Ward
authors.forename: Frank
authors.initials: F
authors.lastname: Sobott
authors.forename: Joseph
authors.initials: J
authors.lastname: Maman
authors.forename: Andal S
authors.initials: AS
authors.lastname: Murthy
authors.forename: Aleksandra A
authors.initials: AA
authors.lastname: Watson
authors.forename: Oleg
authors.initials: O
authors.lastname: Fedorov
authors.forename: Andrew
authors.initials: A
authors.lastname: Bowman
authors.forename: Tom
authors.initials: T
authors.lastname: Owen-Hughes
authors.forename: Hassane
authors.initials: H
authors.lastname: El Mkami
authors.forename: Natalia V
authors.initials: NV
authors.lastname: Murzina
authors.forename: David G
authors.initials: DG
authors.lastname: Norman
authors.forename: Ernest D
authors.initials: ED
authors.lastname: Laue
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002843:Chromatin / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D004247:DNA / Q000378:metabolism; D004261:DNA Replication; D056488:Histone Chaperones / Q000737:chemistry / Q000378:metabolism*; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding; D055503:Protein Multimerization; D056505:Retinoblastoma-Binding Protein 4 / Q000737:chemistry / Q000378:metabolism*
chemical_list: C491640:ASF1B protein, human; D018797:Cell Cycle Proteins; D002843:Chromatin; D056488:Histone Chaperones; D006657:Histones; D009707:Nucleosomes; C082637:RBBP4 protein, human; D056505:Retinoblastoma-Binding Protein 4; D004247:DNA