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Titolo:
Characterization of a chromatin remodelling activity in Xenopus oocytes
Autore:
Gelius, B; Wade, P; Wolffe, A; Wrange, O; Farrants, AKO;
Indirizzi:
Karolinska77nst, Med Nobel Inst, Dept Cell & Mol Biol, Mol Genet Lab, S-171 Karolinska Inst Stockholm Sweden S-17177 Mol Biol, Mol Genet Lab, S-171 Univ Stockholm, Wenner Gren Inst, Dept Cell Biol, S-11345 Stockholm, Sweden Univ Stockholm Stockholm Sweden S-11345 Biol, S-11345 Stockholm, Sweden NICHHD, Mol Embryol Lab, Bethesda, MD 20892 USA NICHHD Bethesda MD USA 20892 HHD, Mol Embryol Lab, Bethesda, MD 20892 USA
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 262, anno: 1999,
pagine: 426 - 434
SICI:
0014-2956(199906)262:2<426:COACRA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR VIRUS PROMOTER; SWI-SNF COMPLEX; SACCHAROMYCES-CEREVISIAE; GLUCOCORTICOID RECEPTOR; DROSOPHILA-BRAHMA; NUCLEOSOME DISRUPTION; SWI/SNF COMPLEX; IN-VITRO; YEAST; TRANSCRIPTION;
Keywords:
BRG1; chromatin; nucleosome remodeling; SWI SNF; Xenopus oocytes; glucocorticoid receptor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Wrange, O Karolinska77nst, Med Nobel Inst, Dept Cell & Mol Biol, Mol GenetLab, S-171 Karolinska Inst Stockholm Sweden S-17177 Mol Genet Lab, S-171
Citazione:
B. Gelius et al., "Characterization of a chromatin remodelling activity in Xenopus oocytes", EUR J BIOCH, 262(2), 1999, pp. 426-434

Abstract

The yeast SWI2/SNF2 protein is a component of a large protein complex which is involved in the remodelling of chromatin during transcriptional activation. Several homologous complexes have been found in Drosophila and mammals. We have examined the expression of the SWI2/SNF2 homologue BRG1 in Xenopus laevis using two antisera originally raised against the C-terminus of the rat and the human BRG1 protein. These two antisera crossreacted with a protein found in both Xenopus liver and Xenopus oocytes. The Xenopus BRG1-like protein is expressed throughout oogenesis (stages I-VI) and embryogenesis. By injecting an expression vector containing the full-length human BRG1 cDNA into Xenopus oocytes, the relative molecular weight (M-r) of the Xenopus BRG1-like protein was shown to be slightly lower than that of the human BRG1, 190 000 and 200 000, respectively. The Xenopus BRG1-like protein elutes at a M-r of approximate to 2 000 000 on Superose HR6(TM) size-exclusion chromatography, indicating that it is part of a larger complex, as are all other known SWI/SNF proteins. Nucleosome remodelling activity was co-eluted with the BRG1 immunogenic activity in both ion-exchange and size-exclusion chromatography.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 11:56:04