A SINGLE-STRANDED DNA-BINDING PROTEIN PROMOTES THE BINDING OF THE PURIFIED ESTROGEN-RECEPTOR TO ITS RESPONSIVE ELEMENT

被引：109

作者：

MUKHERJEE, R ^{[1
]}

CHAMBON, P ^{[1
]}

机构：

[1] FAC MED STRASBOURG,INST CHIM BIOL,CNRS,GENET MOLEC EUCARYOTES LAB,INSERM,U184,11 RUE HUMANN,F-67085 STRASBOURG,FRANCE

来源：

NUCLEIC ACIDS RESEARCH | 1990年 / 18卷 / 19期

关键词：

D O I：

10.1093/nar/18.19.5713

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 purified human oestrogen receptor (hER) does not form a detectable complex with an oestrogen responsive element (ERE) under conditions where hER-ERE complexes are readily formed with crude extracts from Hela or yeast cells expressing the hER. This Indicates that other factor(s) are necessary for ER-ERE binding. Such a ER DNA binding stimulatory factor (DBSF) has been purified from the yeast Saccharomyces cerevislae. It is a 45 kDa single-stranded DNA-binding protein (SSB) which cannot be substituted for by the purified E.coi SSB. © 1990 Oxford University Press.

引用

页码：5713 / 5716

页数：4

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