Characterization of a chromatin remodelling activity in Xenopus oocytes

被引:21
作者
Gelius, B
Wade, P
Wolffe, A
Wrange, Ö [1 ]
Farrants, AKÖ
机构
[1] Karolinska Inst, Med Nobel Inst, Dept Cell & Mol Biol, Mol Genet Lab, S-17177 Stockholm, Sweden
[2] Univ Stockholm, Wenner Gren Inst, Dept Cell Biol, S-11345 Stockholm, Sweden
[3] NICHHD, Mol Embryol Lab, Bethesda, MD 20892 USA
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1999年 / 262卷 / 02期
关键词
BRG1; chromatin; nucleosome remodeling; SWI SNF; Xenopus oocytes; glucocorticoid receptor;
D O I
10.1046/j.1432-1327.1999.00379.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:426 / 434
页数:9
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