In vivo footprinting of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific factor

doi:10.1016/0092-8674(91)90370-E

Cell

Volume 67, Issue 5, 29 November 1991, Pages 977-986

https://doi.org/10.1016/0092-8674(91)90370-E Get rights and content

Abstract

HNF5, a liver-specific DNA-binding protein, interacts with DNA in a manner that allows DNAase I cleavage in the middle of its recognition sequence. Using this property we have identified in vivo HNF5 bound to its sites within two glucocorticoid-responsive units of the rat tyrosine aminotransferase (TAT) gene. One HNF5-binding site is also a glucocorticoid receptor-binding site; glucocorticoid-dependent HNF5 binding could be detected at this site even though it is incompatible with glucocorticoid receptor binding. HNF5 binds within 10 min of hormone addition, indicating that it participates in transcriptional activation. In the TAT gene glucocorticoid-dependent HNF5 binding occurs where there is glucocorticoid-dependent disruption of nucleosomal structure; constitutive binding occurs in constitutively disrupted regions. These results suggest a hit-and-run mechanism of transcriptional activation by glucocorticoid receptor: the activated receptor binds its target sequence, modifies local chromatin structure, then leaves its site accessible to another factor.

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Cell

ArticleIn vivo footprinting of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific factor

Abstract

Cell

Cell

Cell

Meth. Enzymol.

Cell

Cell

J. Biol. Chem.

Cell

Cell

Cell

Cell

Cooperative interaction of chicken lysozyme enhancer subdomains partially overlapping with a steroid receptor binding site

Nucl. Acids Res.

Transcription factor access is mediated by accurately positioned nucleosomes on the mouse mammary tumor virus promoter

Mol. Cell. Biol.

Estrogen-inducible binding of a nuclear factor to the vitellogenin upstream region

Mol. Cell. Biol.

Tissue-specific DNAse I hypersensitive sites in the 5′-flanking sequences of the tryptophan oxygenase and the tyrosine aminotransferase genes

EMBO J.

In vivo protein-DNA interactions in a glucocorticoid response element require the presence of the hormone

Nature

Nuclear factor-I acts as a transcription factor on the MMTV promoter but competes with steroid hormone receptors for DNA binding

EMBO J.

Glucocorticoids locally disrupt an array of positioned nucleosomes on the rat tyrosine aminotransferase promoter in hepatoma cells

Steroid receptor family: structure and functions

Binding of multiple factors to the MMTV promoter in crude and fractionated nuclear extracts

Article
In vivo footprinting of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific factor