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5. Effect of ligand binding and DNA binding on the structure of the mouse oestrogen receptor.

Author

Emmas CE, Fawell SE, Hoare SA, and Parker MG

Subjects
Animals, Baculoviridae genetics, Base Sequence, Binding Sites, Binding, Competitive, Cell Line, DNA-Binding Proteins drug effects, Endopeptidases, Estrogen Antagonists pharmacology, Kinetics, Ligands, Mice, Molecular Sequence Data, Peptide Mapping, Polyunsaturated Alkamides, Receptors, Estrogen drug effects, Receptors, Estrogen genetics, Recombinant Proteins metabolism, Regulatory Sequences, Nucleic Acid, Tamoxifen pharmacology, Transfection, DNA-Binding Proteins metabolism, Estradiol analogs & derivatives, Estradiol pharmacology, Receptors, Estrogen metabolism, Tamoxifen analogs & derivatives
Abstract

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.

Published
1992
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