title: Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding.
abstract: Here we have examined HIV-1 nucleosome remodeling upon the binding of transcription factors and the SWI/SNF complex using a novel approach. The approach combines UV laser protein-DNA crosslinking, electrophoretic mobility-shift analysis and DNase I protection analysis with immunochemical techniques. It was found that single activator-bound HIV-1 nucleosomes exhibit very weak perturbation in histone NH(2) tail-DNA interactions. However, the simultaneous binding of the transcription activators Sp1, NF-kB1, LEF-1 and USF synergistically increased the release of histone NH(2) tails from nucleosomal DNA. In contrast, the binding of SWI/SNF complex to HIV-1 nucleosome disrupted structured histone domain-DNA contacts, but not histone NH(2) tail-DNA interactions. Stable remodeled nucleosomes, (obtained after detachment of SWI/SNF), displayed identical structural alterations with those bound to SWI/SNF. These results demonstrate a different in vitro remodeling of the HIV-1 nucleosome upon the binding of multiple transcription activators and of SWI/SNF complex.
authors.affiliation: Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, équipe Mécanismes d'Assemblage du Matériel Génétique, INSERM U 309, France.
authors.forename: D
authors.initials: D
authors.lastname: Angelov
authors.forename: M
authors.initials: M
authors.lastname: Charra
authors.forename: M
authors.initials: M
authors.lastname: Seve
authors.forename: J
authors.initials: J
authors.lastname: Côté
authors.forename: S
authors.initials: S
authors.lastname: Khochbin
authors.forename: S
authors.initials: S
authors.lastname: Dimitrov
mesh_terms: D018983:DNA Footprinting; D004265:DNA Helicases; D004279:DNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D003850:Deoxyribonuclease I / Q000378:metabolism; D015967:Gene Expression Regulation, Viral; D015497:HIV-1 / Q000235:genetics*; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007834:Lasers; D051821:Lymphoid Enhancer-Binding Factor 1; D046911:Macromolecular Substances; D016328:NF-kappa B / Q000378:metabolism; D009687:Nuclear Proteins; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011233:Precipitin Tests; D011485:Protein Binding; D016329:Sp1 Transcription Factor / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic / Q000235:genetics; D014466:Ultraviolet Rays; D051720:Upstream Stimulatory Factors
chemical_list: D004279:DNA, Viral; D004268:DNA-Binding Proteins; D006657:Histones; C497573:LEF1 protein, human; D051821:Lymphoid Enhancer-Binding Factor 1; D046911:Macromolecular Substances; D016328:NF-kappa B; D009687:Nuclear Proteins; D009707:Nucleosomes; C499336:SMARCA1 protein, human; C084011:SMARCA2 protein, human; D016329:Sp1 Transcription Factor; D015534:Trans-Activators; D014157:Transcription Factors; C497181:USF1 protein, human; D051720:Upstream Stimulatory Factors; D003850:Deoxyribonuclease I; C084108:SMARCA4 protein, human; D004265:DNA Helicases