Antiestrogen-liganded estrogen receptor interaction with estrogen responsive element DNA in vitro

1992 ◽  
Vol 43 (4) ◽  
pp. 249-262 ◽  
Author(s):  
Carolyn M. Klinge ◽  
Robert A. Bambara ◽  
Russell Hilf
Keyword(s):  
Estrogen Receptor ◽  
Receptor Interaction ◽  
Estrogen Responsive Element ◽  
Responsive Element

scholarly journals An Explanation for Observed Estrogen Receptor Binding to Single-Stranded Estrogen-Responsive Element DNA

1999 ◽  
Vol 13 (6) ◽  
pp. 958-968 ◽  
Author(s):  
Mark D. Driscoll ◽  
Ganesan Sathya ◽  
Layla F. Saidi ◽  
Michael S. DeMott ◽  
Russell Hilf ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Binding Mode ◽  
Single Strand ◽  
Estrogen Response ◽  
Estrogen Responsive Element ◽  
Receptor Action ◽  
Responsive Element ◽  
Inducible Genes

Abstract Estrogen-inducible genes contain an enhancer called the estrogen response element (ERE), a double-stranded inverted repeat. The estrogen receptor (ER) is generally thought to bind to the double-stranded ERE. However, some reports provide evidence that an ER homodimer can bind a single strand of the ERE and suggest that single-stranded ERE binding is the preferred binding mode for ER. Since these two models describe quite different mechanisms of receptor action, we have attempted to reconcile the observations. Analyzing DNA structure by nuclease sensitivity, we found that two identical molecules of a single strand of DNA containing the ERE sequence can partially anneal in an antiparallel manner. Bimolecular annealing produces double-stranded inverted repeats, with adjacent unannealed tails. The amount of annealing correlates exactly with the ability of ER to bind bimolecular EREs. Either strand of an ERE could anneal to itself in a way that would bind ER. We conclude that ER binds only the annealed double-stranded ERE both in vitro and in vivo.

scholarly journals A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor

1988 ◽  
Vol 16 (2) ◽  
pp. 647-663 ◽  
Author(s):  
Ludger Klein-Hitpass ◽  
Gerhart U. Ryffel ◽  
Ellen Heitlinger ◽  
Andrew C.B. Cato
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Responsive Element ◽  
Responsive Element

scholarly journals SPBP Is a Phosphoserine-Specific Repressor of Estrogen Receptor α

2005 ◽  
Vol 25 (9) ◽  
pp. 3421-3430 ◽  
Author(s):  
Valentina Gburcik ◽  
Nathalie Bot ◽  
Marcello Maggiolini ◽  
Didier Picard
Keyword(s):  
Estrogen Receptor ◽  
Activation Function ◽  
Estrogen Receptor Α ◽  
Fine Tuning ◽  
Breast Cancer Cell Lines ◽  
Interaction Domain ◽  
Phosphorylated Form ◽  
Element Binding Protein ◽  
Responsive Element

ABSTRACT Multiple signaling pathways stimulate the activity of estrogen receptor α (ERα) by direct phosphorylation within its N-terminal activation function 1 (AF1). How phosphorylation affects AF1 activity remains poorly understood. We performed a phage display screen for human proteins that are exclusively recruited to the phosphorylated form of AF1 and found the stromelysin-1 platelet-derived growth factor-responsive element-binding protein (SPBP). In a purified system, SPBP bound only the in vitro-phosphorylated form of the ERα AF1 or the phosphoserine mimic S118E, and the interaction domain could be mapped to a 42-amino-acid fragment of SPBP. In cells, SPBP preferentially interacted with liganded and phosphorylated ERα. Functionally, SPBP behaved as a repressor of activated ERα, which extends its previously demonstrated roles as a DNA binding transactivation factor and coactivator of other transcription factors. By targeting the phosphorylated form of AF1, SPBP may contribute to attenuating and fine-tuning ERα activity. A functional consequence is that SPBP inhibits the proliferation of ERα-dependent but not ERα-independent breast cancer cell lines, mirroring a reported negative correlation with the ERα status of breast tumors.

scholarly journals In VitroBinding of the Purified Hormone-Binding Subunit of the Estrogen Receptor to Oligonucleotides Containing Natural or Modified Sequences of an Estrogen-Responsive Element

1991 ◽  
Vol 5 (4) ◽  
pp. 555-563 ◽  
Author(s):  
Nicola Medici ◽  
Vincenzo Nigro ◽  
Ciro Abbondanza ◽  
Bruno Moncharmont ◽  
Anna Maria Molinari ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Hormone Binding ◽  
Estrogen Responsive Element ◽  
Responsive Element ◽  
Binding Subunit

Characterization of an estrogen-responsive element implicated in regulation of the rainbow trout estrogen receptor gene

1995 ◽  
Vol 15 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Y Le Dréan ◽  
G Lazennec ◽  
L Kern ◽  
D Saligaut ◽  
F Pakdel ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Rainbow Trout ◽  
Receptor Gene ◽  
Expression System ◽  
Consensus Sequence ◽  
Gene Promoter ◽  
Dnase I Footprinting ◽  
Estrogen Responsive Element ◽  
Responsive Element ◽  
Simplex Virus

ABSTRACT We previously reported that the expression of the rainbow trout estrogen receptor (rtER) gene is markedly increased by estradiol (E2). In this paper, we have used transient transfection assays with reporter plasmids expressing chloramphenicol acetyl transferase (CAT), linked to 5′ flanking regions of the rtER gene promoter, to identify cis-elements responsible for E2 inducibility. Deletion analysis localized an estrogen-responsive element (ERE), at position +242, with one mutation on the first base compared with the consensus sequence. This element confers estrogen responsiveness to CAT reporter linked to both the herpes simplex virus thymidine kinase promoter and the homologous rtER promoter. Moreover, using a 0·2 kb fragment of the rtER promoter encompassing the ERE and the rtER DNA binding domain obtained from a bacterial expression system, DNase I footprinting experiments demonstrated a specific protection covering 20 bp (+240/+260) containing the ERE sequence. Based on these studies, we believe that this ERE sequence, identified in the rtER gene promoter, may be a major cis-acting element involved in the regulation of the gene by estrogen.

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