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PMID: 2792086 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Glucocorticoid receptor binds cooperatively to adjacent recognition sites.

The EMBO journal ·Vol. 8 ·No. 8 ·1989-08-00 ·Pages 2257-63

Schmid W, Strähle U, Schütz G, Schmitt J, Stunnenberg H

Abstract

In order to define the mechanism of synergistic induction mediated by multiple glucocorticoid response elements (GRE), the affinity of the glucocorticoid receptor to a single or duplicated GRE was analyzed by gel retardation, nitrocellulose filter binding and by footprinting experiments. Direct measurement of the relative affinity and indirect determination by competition showed greater than 10-fold higher affinity of the glucocorticoid receptor to a duplicated GRE when compared to a single element. Maximal stability of the GRE-receptor complex was obtained using two closely spaced GREs positioned on the same side of the DNA helix. Increasing the distance or changing the helical position of the GREs considerably increased the off rate of the receptor. DNase I footprinting shows in addition to the protection of the GRE region, an altered pattern in the nonprotected intervening DNA indicating structural alteration of the DNA helix by the receptor bound to adjacent GREs.

MeSH Terms
Animals Autoradiography Base Sequence Binding, Competitive DNA/genetics,metabolism Genetic Vectors Half-Life Humans Male Molecular Sequence Data Nucleic Acid Conformation Rats Receptors, Glucocorticoid/metabolism Vaccinia virus/genetics
Chemicals
Receptors, Glucocorticoid DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Schmid W
Institute of Cell and Tumor Biology, German Cancer Research Center, Heidelberg, FRG.
Strähle U
Schütz G
Schmitt J
Stunnenberg H
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1989-08-00
Pages
2257-63
Language
English
Region
England
NLM ID
8208664
PMCID
PMC401156
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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