Three amino acids of the oestrogen receptor are essential to its ability to distinguish an oestrogen from a glucocorticoid-responsive element
- PMID: 2922054
- DOI: 10.1038/338271a0
Three amino acids of the oestrogen receptor are essential to its ability to distinguish an oestrogen from a glucocorticoid-responsive element
Abstract
Steroid hormone receptors activate specific gene transcription by binding as hormone-receptor complexes to DNA enhancer elements termed hormone responsive elements. A highly conserved 66-amino-acid region of the oestrogen and glucocorticoid receptors which corresponds to part of the receptor DNA-binding domain (region C) determines the specificity of target gene recognition. This region contains two subregions (CI and CII), encoded in two separate exons, that are analogous to the 'zinc fingers' of the transcription factor TFIIIA. The N-terminal CI finger determines the recognition specificity of the hormone responsive element. A chimaeric oestrogen receptor, in which the CI finger is replaced with the corresponding glucocorticoid receptor CI finger region, activates transcription from a reporter gene containing a glucocorticoid-responsive element, but not from a reporter gene containing an oestrogen-responsive element. We report here that three amino acids located at the C-terminal side of the oestrogen receptor CI finger play a key part in this specificity.
Similar articles
-
Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor.Nature. 1987 Jan 1-7;325(6099):75-8. doi: 10.1038/325075a0. Nature. 1987. PMID: 3025750
-
Chimeric receptors used to probe the DNA-binding domain of the estrogen and glucocorticoid receptors.Cancer Res. 1989 Apr 15;49(8 Suppl):2282s-2285s. Cancer Res. 1989. PMID: 2702667
-
The N-terminal DNA-binding 'zinc finger' of the oestrogen and glucocorticoid receptors determines target gene specificity.EMBO J. 1988 Oct;7(10):3037-44. doi: 10.1002/j.1460-2075.1988.tb03168.x. EMBO J. 1988. PMID: 3141145 Free PMC article.
-
Solution structure of the DNA-binding domain of the oestrogen receptor.Nature. 1990 Nov 29;348(6300):458-61. doi: 10.1038/348458a0. Nature. 1990. PMID: 2247153
-
Modulation of oestrogen receptor activity by oestrogens and anti-oestrogens.J Steroid Biochem Mol Biol. 1990 Dec 20;37(6):747-51. doi: 10.1016/0960-0760(90)90415-h. J Steroid Biochem Mol Biol. 1990. PMID: 2285586 Review.
Cited by
-
Eukaryotic glucose-6-phosphate dehydrogenases: structural screening of related proteins.J Protein Chem. 1991 Feb;10(1):25-9. doi: 10.1007/BF01024652. J Protein Chem. 1991. PMID: 2054059
-
The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1.Mol Cell Biol. 1990 Oct;10(10):5128-37. doi: 10.1128/mcb.10.10.5128-5137.1990. Mol Cell Biol. 1990. PMID: 2118990 Free PMC article.
-
Estrogen receptor interaction with estrogen response elements.Nucleic Acids Res. 2001 Jul 15;29(14):2905-19. doi: 10.1093/nar/29.14.2905. Nucleic Acids Res. 2001. PMID: 11452016 Free PMC article. Review.
-
A mutation in the DNA-binding domain of the androgen receptor gene causes complete testicular feminization in a patient with receptor-positive androgen resistance.J Clin Invest. 1991 Mar;87(3):1123-6. doi: 10.1172/JCI115076. J Clin Invest. 1991. PMID: 1999491 Free PMC article.
-
Defining a minimal estrogen receptor DNA binding domain.Nucleic Acids Res. 1993 Mar 11;21(5):1125-32. doi: 10.1093/nar/21.5.1125. Nucleic Acids Res. 1993. PMID: 8385312 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources