title: A basic domain in the histone H2B N-terminal tail is important for nucleosome assembly by FACT.
abstract: Nucleosome assembly in vivo requires assembly factors, such as histone chaperones, to bind to histones and mediate their deposition onto DNA. In yeast, the essential histone chaperone FACT (FAcilitates Chromatin Transcription) functions in nucleosome assembly and H2A-H2B deposition during transcription elongation and DNA replication. Recent studies have identified candidate histone residues that mediate FACT binding to histones, but it is not known which histone residues are important for FACT to deposit histones onto DNA during nucleosome assembly. In this study, we report that the histone H2B repression (HBR) domain within the H2B N-terminal tail is important for histone deposition by FACT. Deletion of the HBR domain causes significant defects in histone occupancy in the yeast genome, particularly at HBR-repressed genes, and a pronounced increase in H2A-H2B dimers that remain bound to FACT in vivo Moreover, the HBR domain is required for purified FACT to efficiently assemble recombinant nucleosomes in vitro We propose that the interaction between the highly basic HBR domain and DNA plays an important role in stabilizing the nascent nucleosome during the process of histone H2A-H2B deposition by FACT.
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Peng
authors.initials: P
authors.lastname: Mao
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: McKenna N M
authors.initials: MN
authors.lastname: Kyriss
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Amelia J
authors.initials: AJ
authors.lastname: Hodges
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Mingrui
authors.initials: M
authors.lastname: Duan
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Robert T
authors.initials: RT
authors.lastname: Morris
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Mark D
authors.initials: MD
authors.lastname: Lavine
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Traci B
authors.initials: TB
authors.lastname: Topping
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA.
authors.forename: Lisa M
authors.initials: LM
authors.lastname: Gloss
authors.affiliation: School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA jwyrick@wsu.edu.
authors.forename: John J
authors.initials: JJ
authors.lastname: Wyrick
mesh_terms: D000818:Animals; D002470:Cell Survival / Q000235:genetics; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004275:DNA, Ribosomal / Q000737:chemistry / Q000378:metabolism; D005786:Gene Expression Regulation; D016678:Genome; D056488:Histone Chaperones / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D012341:RNA, Ribosomal, 5S / Q000235:genetics; D011994:Recombinant Proteins; D017384:Sequence Deletion
chemical_list: D004275:DNA, Ribosomal; D056488:Histone Chaperones; D006657:Histones; D009707:Nucleosomes; D012341:RNA, Ribosomal, 5S; D011994:Recombinant Proteins; D004247:DNA