title: 2,3,7,8-Tetrachlorodibenzo-p-dioxin-inducible aryl hydrocarbon receptor-mediated change in CYP1A1 chromatin structure occurs independently of transcription.
abstract: 2,3,7,8-Tetrachlorodibenzo-p-dioxin induces, in a receptor-dependent fashion, an increase in the accessibility of CYP1A1 chromatin to restriction endonucleases. The 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced change in chromatin structure occurs rapidly and does not require ongoing RNA or protein synthesis. The increased accessibility of chromatin DNA may facilitate its subsequent interaction with other transcription factors.
authors.affiliation: Department of Pharmacology, Stanford University School of Medicine, California 94305.
authors.forename: L K
authors.initials: LK
authors.lastname: Durrin
authors.forename: J P
authors.initials: JP
authors.lastname: Whitlock
mesh_terms: D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism; D002843:Chromatin / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D003513:Cycloheximide / Q000494:pharmacology; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics*; D003609:Dactinomycin / Q000494:pharmacology; D004147:Dioxins / Q000494:pharmacology*; D005796:Genes; D006838:Hydrocarbons / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000235:genetics / Q000378:metabolism; D051379:Mice; D009154:Mutation; D000072317:Polychlorinated Dibenzodioxins / Q000494:pharmacology*; D012333:RNA, Messenger / Q000235:genetics; D018336:Receptors, Aryl Hydrocarbon; D011955:Receptors, Drug / Q000235:genetics; D015183:Restriction Mapping; D014158:Transcription, Genetic / Q000187:drug effects; D014444:Tyrosine Transaminase / Q000235:genetics
chemical_list: D002843:Chromatin; D004147:Dioxins; D006838:Hydrocarbons; D000072317:Polychlorinated Dibenzodioxins; D012333:RNA, Messenger; D018336:Receptors, Aryl Hydrocarbon; D011955:Receptors, Drug; D003609:Dactinomycin; D003577:Cytochrome P-450 Enzyme System; D003513:Cycloheximide; D014444:Tyrosine Transaminase