EFFECT OF LIGAND-BINDING AND DNA-BINDING ON THE STRUCTURE OF THE MOUSE ESTROGEN-RECEPTOR

被引:13
作者
EMMAS, CE [1 ]
FAWELL, SE [1 ]
HOARE, SA [1 ]
PARKER, MG [1 ]
机构
[1] IMPERIAL CANC RES FUND,MOLEC ENDOCRINOL LAB,LINCOLNS INN FIELDS,LONDON WC2A 3PX,ENGLAND
关键词
D O I
10.1016/0960-0760(92)90354-L
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
We have investigated the effects of ligand and DNA binding on the structure of the oestrogen receptor by performing limited proteolysis and analysing DNA binding activity by gel shift analysis. The effects of oestradiol, 4-hydroxytamoxifen and ICI 164,384 have been examined and we have found that despite differences in the DNA binding activity or relative mobility of the receptor-DNA complex we were unable to detect differences in the cleavage pattern produced by trypsin, chymotrypsin, Staphylococcus aureus V8, papain or elastase. Inhibition of DNA binding by ICI 164,384 was lost in receptor fragments that lacked the hormone binding domain. In contrast to the full-length receptor, proteolytic fragments produced by chymotrypsin differed in their ability to bind to an oestrogen response element (ERE) vs a thyroid response element (TRE). Evidence is presented that this difference can be accounted for by the inability of fragments lacking the hormone binding domain to dimerise on a TRE.
引用
收藏
页码:291 / 299
页数:9
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