Glucocorticoid receptor binds cooperatively to adjacent recognition sites

W. Schmid, U. Strahle, G. Schutz, J. Schmitt, H. Stunnenberg

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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 > 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.

Original languageEnglish
Pages (from-to)2257-2263
Number of pages7
JournalEMBO Journal
Issue number8
Publication statusPublished - 1989
Externally publishedYes


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