Open AccessInteraction of Rat‐Liver Glucocorticoid Receptor with DNA
Author(s) -
MILGROM Edwin,
ATGER Michel,
BAILLY Alain
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10948.x
Subject(s) - glucocorticoid receptor , dna , divalent , receptor , steroid , ionic strength , steroid hormone , liver cell , biology , biochemistry , glucocorticoid , binding site , microbiology and biotechnology , chemistry , hormone , endocrinology , medicine , aqueous solution , organic chemistry
The complex of [ 3 H]dexamethasone and rat liver receptor binds to rat liver DNA. This interaction takes place only in the presence of hormone and is enhanced by ‘activation’. No evidence of saturatability can be obtained with concentrations of steroid‐receptor complexes corresponding to those observed physiologically in the intact liver cell. The binding is inhibited by high ionic strength and by millimolar concentrations of divalent cations. No species specificity has been observed: the complex binds equally well to prokaryotic and eukaryotic DNA's. There was no difference between binding to native and denatured DNA. In comparable conditions twice as much [ 3 H]dexamethasonereceptor complexes were bound by DNA than by rat liver nuclei. Thus, the interaction of steroid‐receptor complexes with DNA probably does not correspond to the recognition of a few very specific sequences. It is however possible that this interaction is actually operating in vivo in the intact cell.