Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Roles of the histone H2A-H2B dimers and the (H3-H4)(2) tetramer in nucleosome remodeling by the SWI-SNF complex
Autore:
Boyer, LA; Shao, X; Ebright, RH; Peterson, CL;
Indirizzi:
Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA UnivMassachusetts Worcester MA USA 01605 ol Med, Worcester, MA 01605 USA Univ Massachusetts, Sch Med, Dept Biochem & Mol Biol, Worcester, MA 01605 USA Univ Massachusetts Worcester MA USA 01605 l Biol, Worcester, MA 01605 USA Rutgers State Univ, Waksman Inst, Howard Hughes Med Inst, Piscataway, NJ 08854 USA Rutgers State Univ Piscataway NJ USA 08854 Inst, Piscataway, NJ 08854 USA Rutgers State Univ, Dept Chem, Piscataway, NJ 08854 USA Rutgers State Univ Piscataway NJ USA 08854 Chem, Piscataway, NJ 08854 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 16, volume: 275, anno: 2000,
pagine: 11545 - 11552
SICI:
0021-9258(20000421)275:16<11545:ROTHHD>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST SWI/SNF COMPLEX; ACTIVE DNA-SEQUENCES; CORE PARTICLE; TRANSCRIPTIONAL ACTIVATORS; TRANSCRIBING CHROMATIN; RNA GENE; BINDING; ARRAYS; OCTAMER; RECRUITMENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Peterson, CL Univ Massachusetts, Sch Med, Program Mol Med, 373 Plantat St,Biotech 2,Suite 301, Worcester, MA 01605 USA Univ Massachusetts 373 PlantatSt,Biotech 2,Suite 301 Worcester MA USA 01605
Citazione:
L.A. Boyer et al., "Roles of the histone H2A-H2B dimers and the (H3-H4)(2) tetramer in nucleosome remodeling by the SWI-SNF complex", J BIOL CHEM, 275(16), 2000, pp. 11545-11552

Abstract

SWI-SNF is an ATP-dependent chromatin remodeling complex required for expression of a number of yeast genes. Previous studies have suggested that SWI-SNF action may remove or rearrange the histone H2A-H2B dimers or induce a novel alteration in the histone octamer. Here, we have directly tested these and other models by quantifying the remodeling activity of SWI-SNF on arrays of (H3-H4)(2) tetramers, on nucleosomal arrays reconstituted with disulfide-linked histone H3, and on arrays reconstituted with histone H3 derivatives site-specifically modified at residue 110 with the fluorescent probe acetylethylenediamine-(1,5)-naphthol sulfonate, We find that SWI-SNF can remodel (H3-H4)(2) tetramers, although tetramers are poor substrates for SWI-SNF remodeling compared with nucleosomal arrays. SWI-SNF can also remodel nucleosomal arrays that harbor disulfide-linked (H3-H4)(2) tetramers, indicating that SWI-SNF action does not involve an obligatory disruption of the tetramer, Finally, we find that although the fluorescence emission intensity of acetylethylenediamine-(1,5)-naphthol sulfonate-modified histone H3 is sensitive to octamer structure, SWI-SNF action does not alter fluorescence emission intensity. These data suggest that perturbation of the histone octamer is not a requirement or a consequence of ATP-dependent nucleosome remodeling by SWI-SNF.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 12:15:23