In vivo protein–DNA interactions in a glucocorticoid response element require the presence of the hormone View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1986-12

AUTHORS

Peter B. Becker, Bernd Gloss, Wolfgang Schmid, Uwe Strähle, Günther Schütz

ABSTRACT

Transcriptional activation of gene expression by glucocorticoid hormones is mediated by the interaction of hormone-receptor complexes with specific DNA sequences called glucocorticoid responsive elements (GREs) (refs 1-3, see ref. 4 for review). Deletion of this sequence abolishes glucocorticoid induction of transcription. According to a current model, activation of the cytoplasmic receptor protein by hormone binding leads to its increased affinity for and translocation to the nucleus. However, recent reports that the oestradiol and progesterone receptors are localized in the nucleus in the absence of steroid led us to examine whether the free receptor interacts in vivo with its DNA binding site in the absence of hormone binding. We used the genomic footprinting technique to show that changes in in vivo protein-DNA interactions within the GREs of the tyrosine aminotransferase gene (TAT) can be detected only after hormone treatment in hepatoma cells. Such changes are not detected in fibroblast cells, in which the TAT gene is not expressed. Many of the changes in dimethylsulphate reactivity observed in the living cell are also found in vitro using cloned DNA and a partially purified glucocorticoid receptor. More... »

PAGES

686-688

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/324686a0

DOI

http://dx.doi.org/10.1038/324686a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025011269

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2879246


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