title: Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes.
abstract: Remodeling machines play an essential role in the control of gene expression, but how their activity is regulated is not known. Here we report that the nuclear protein nucleolin possesses a histone chaperone activity and that this factor greatly enhances the activity of the chromatin remodeling machineries SWI/SNF and ACF. Interestingly, nucleolin is able to induce the remodeling by SWI/SNF of macroH2A, but not of H2ABbd nucleosomes, which are otherwise resistant to remodeling. This new histone chaperone promotes the destabilization of the histone octamer, helping the dissociation of a H2A-H2B dimer, and stimulates the SWI/SNF-mediated transfer of H2A-H2B dimers. Furthermore, nucleolin facilitates transcription through the nucleosome, which is reminiscent of the activity of the FACT complex. This work defines new functions for histone chaperones in chromatin remodeling and regulation of transcription and explains how nucleolin could act on transcription.
authors.affiliation: Ecole Normale Supérieure de Lyon, CNRS-UMR 5161/INRA 1237/IFR128 Biosciences, Lyon-Gerland, France.
authors.forename: Dimitar
authors.initials: D
authors.lastname: Angelov
authors.forename: Vladimir A
authors.initials: VA
authors.lastname: Bondarenko
authors.forename: Sébastien
authors.initials: S
authors.lastname: Almagro
authors.forename: Hervé
authors.initials: H
authors.lastname: Menoni
authors.forename: Fabien
authors.initials: F
authors.lastname: Mongélard
authors.forename: Fabienne
authors.initials: F
authors.lastname: Hans
authors.forename: Flore
authors.initials: F
authors.lastname: Mietton
authors.forename: Vasily M
authors.initials: VM
authors.lastname: Studitsky
authors.forename: Ali
authors.initials: A
authors.lastname: Hamiche
authors.forename: Stefan
authors.initials: S
authors.lastname: Dimitrov
authors.forename: Philippe
authors.initials: P
authors.lastname: Bouvet
mesh_terms: D000818:Animals; D042002:Chromatin Assembly and Disassembly; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000502:physiology*; D019281:Dimerization; D006609:High Mobility Group Proteins / Q000502:physiology*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D009707:Nucleosomes / Q000378:metabolism / Q000502:physiology*; D010750:Phosphoproteins / Q000502:physiology*; D021381:Protein Transport; D012319:RNA Polymerase II / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000502:physiology*; D014157:Transcription Factors / Q000378:metabolism; D015533:Transcriptional Activation; D035602:Transcriptional Elongation Factors / Q000502:physiology*; D014982:Xenopus laevis; D000097796:Nucleolin
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes; D010750:Phosphoproteins; D012319:RNA Polymerase II; D016601:RNA-Binding Proteins; D014157:Transcription Factors; D035602:Transcriptional Elongation Factors; D000097796:Nucleolin; C073537:SSRP1 protein, human; C445179:SWI-SNF-B chromatin-remodeling complex