Cooperative binding of steroid hormone receptors contributes to transcriptional synergism at target enhancer elements
CellPublished 1 May 1989
Sophia Y. Tsai, Ming‐Jer Tsai, Bert W. O’Malley
Citations269
SJR quartileQ1
SJR score22.61
SNIP7.62
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TL;DR
The observed synergistic induction of TK-CAT may result from cooperative binding of receptor dimers to the two GRE/PRE sites, as Binding studies demonstrated that occupation of oneGRE/PRE site by a progesterone receptor dimer increased the binding affinity of receptors for the second GRE/ PRE site 100-fold.
Abstract
We demonstrated previously that two molecules of steroid hormone receptor bound efficiently to a single hormone response element (GRE/PRE) of the tyrosine aminotransferase gene (Tsai et al., 1988). Here, we show that two tandemly linked GRE/PREs conferred progesterone inducibility synergistically to a heterologous TK-CAT fusion gene. Binding studies demonstrated that occupation of one GRE/PRE site by a progesterone receptor dimer increased the binding affinity of receptors for the second GRE/PRE site 100-fold. Thus, the observed synergistic induction of TK-CAT may result from cooperative binding of receptor dimers to the two GRE/PRE sites.
Keywords
Immunology and MicrobiologyBiochemistry, Genetics and Molecular Biology
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