title: Histone H2A ubiquitination does not preclude histone H1 binding, but it facilitates its association with the nucleosome.
abstract: Histone H2A ubiquitination is a bulky posttranslational modification that occurs at the vicinity of the binding site for linker histones in the nucleosome. Therefore, we took several experimental approaches to investigate the role of ubiquitinated H2A (uH2A) in the binding of linker histones. Our results showed that uH2A was present in situ in histone H1-containing nucleosomes. Notably in vitro experiments using nucleosomes reconstituted onto 167-bp random sequence and 208-bp (5 S rRNA gene) DNA fragments showed that ubiquitination of H2A did not prevent binding of histone H1 but it rather enhanced the binding of this histone to the nucleosome. We also showed that ubiquitination of H2A did not affect the positioning of the histone octamer in the nucleosome in either the absence or the presence of linker histones.
authors.affiliation: Biacore Incorporated, Piscataway, New Jersey 08854, USA.
authors.forename: Laure J M
authors.initials: LJ
authors.lastname: Jason
authors.forename: Ron M
authors.initials: RM
authors.lastname: Finn
authors.forename: George
authors.initials: G
authors.lastname: Lindsey
authors.forename: Juan
authors.initials: J
authors.lastname: Ausió
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism; D002645:Chickens; D002843:Chromatin / Q000378:metabolism; D002875:Chromosomes / Q000737:chemistry; D004247:DNA / Q000737:chemistry; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000378:metabolism; D006657:Histones / Q000737:chemistry*; D008958:Models, Molecular; D009154:Mutation; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D025801:Ubiquitin; D004247:DNA