title: Effect of in vivo histone hyperacetylation on the state of chromatin fibers.
abstract: We evaluated the contribution of in vivo histone acetylation to the folding of chromatin into its higher-order structures. We have compared high-order folding patterns of hyperacetylated vs. unmodified chromatin in living green monkey kidney cells (CV1 line) using intercalator chloroquine diphospate to induce alterations in the twist of internucleosomal linker DNA. We have shown that histone hyperacetylation induced by antibiotic Trichostatin A significantly alters intercalator-mediated chromatin folding pattern.
authors.affiliation: Institute of Developmental Biology, Russian Academy of Sciences, Moscow. krajewski@ibrran.msk.su
authors.forename: W A
authors.initials: WA
authors.lastname: Krajewski
mesh_terms: D000107:Acetylation; D000818:Animals; D002478:Cells, Cultured; D002738:Chloroquine / Q000494:pharmacology; D002843:Chromatin / Q000737:chemistry*; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000494:pharmacology; D000882:Haplorhini; D006657:Histones / Q000737:chemistry*; D006877:Hydroxamic Acids / Q000494:pharmacology; D007364:Intercalating Agents / Q000494:pharmacology; D007668:Kidney / Q000737:chemistry; D008954:Models, Biological; D010447:Peptide Hydrolases / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
chemical_list: D002843:Chromatin; D004791:Enzyme Inhibitors; D006657:Histones; D006877:Hydroxamic Acids; D007364:Intercalating Agents; C012589:trichostatin A; D002738:Chloroquine; D010447:Peptide Hydrolases; D014357:Trypsin