title: Histone H2A mobility is regulated by its tails and acetylation of core histone tails.
abstract: Histone tail domains play important roles in cellular processes, such as replication, transcription, and chromosome condensation. Histone H2A has one central and two tail domains, and their functions have mainly been studied from a biochemical perspective. In addition, analyses based on visualization have been employed for functional analysis of some chromatin proteins. In this study, we analyzed histone H2A mobility in vivo by two-photon FRAP, and elucidated that the histone H2A N- and C-terminal tails regulate its mobility. We found that histone H2A mobility was increased following treatment of host cells with a histone deacetylase inhibitor. Our results support a model in which core histone tails directly regulate transcription by interacting with nucleosome DNA via electrostatic interactions.
authors: Department of Biotechnology, Graduate School of Engineering, Osaka University, Yamadaoka 2-1, Suita, Osaka 567-0871, Japan.
authors: Tsunehito
authors: T
authors: Higashi
authors: Sachihiro
authors: S
authors: Matsunaga
authors: Keisuke
authors: K
authors: Isobe
authors: Akihiro
authors: A
authors: Morimoto
authors: Tomoko
authors: T
authors: Shimada
authors: Shogo
authors: S
authors: Kataoka
authors: Wataru
authors: W
authors: Watanabe
authors: Susumu
authors: S
authors: Uchiyama
authors: Kazuyoshi
authors: K
authors: Itoh
authors: Kiichi
authors: K
authors: Fukui
mesh_terms: D000107:Acetylation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D036681:Fluorescence Recovery After Photobleaching / Q000379:methods*; D019084:Fluorescent Antibody Technique, Indirect; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D056572:Histone Deacetylase Inhibitors; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology; D015151:Immunoblotting; D009154:Mutation; D021381:Protein Transport / Q000187:drug effects; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013997:Time Factors; D014162:Transfection
chemical_list: D004791:Enzyme Inhibitors; D056572:Histone Deacetylase Inhibitors; D006657:Histones; D006877:Hydroxamic Acids; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; C012589:trichostatin A