Title: Modulation of the estrogen receptor's affinity for DNA by estradiol.

Authors: Skafar, D F; Notides, A C

Published In J Biol Chem, (1985 Oct 05)

Abstract: The binding constant for estrogen receptor-DNA interaction when measured in the presence and absence of estradiol revealed a distinct difference dependent upon whether the receptor was hormone-bound or hormone-free. The binding constant of estrogen receptor-DNA interaction was determined by analysis of the exponential elution profile of the estrogen receptor from DNA-Sepharose columns using Tris buffer at a constant salt concentration. The binding constant of the hormone-bound estrogen receptor for DNA in Tris buffer, pH 7.4, containing 0.2 M KCl was 10.1 +/- 0.8 X 10(6) M-1, 5-fold higher than the value for the hormone-free estrogen receptor. Analysis of the number of ionic bonds between the estrogen receptor and DNA indicates that the hormone-free receptor establishes eight salt bridges, while the hormone-bound estrogen receptor establishes 10-13. The affinity of the hormone-bound estrogen receptor for DNA in Tris buffer at pH 7.4 in 0.2 M KCl is 10-fold greater than at pH 8.0, suggesting that ionic bonding between the receptor and DNA may involve histidine residues of the receptor. The concentration-dependence of the hormone-bound receptor's affinity for DNA emphasizes the receptor's associative state as an influence on the receptor's DNA binding characteristics. Our results demonstrate that estradiol modifies the conformation of the estrogen receptor to a state having an increased affinity for DNA.

PubMed ID: 3840166

MeSH Terms: No MeSH terms associated with this publication