In vivo footprinting of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific factor
Identifieur interne : 000388 ( France/Analysis ); précédent : 000387; suivant : 000389In vivo footprinting of rat TAT gene: Dynamic interplay between the glucocorticoid receptor and a liver-specific factor
Auteurs : Gildas Rigaud [France] ; Jeanne Roux [France] ; Raymond Pictet [France] ; Thierry Grange [France]Source :
- Cell [ 0092-8674 ] ; 1991.
English descriptors
- Teeft :
- Aminotransferase, Beato, Becker, Binding site, Binding sites, Chromatin, Chromatin structure, Cleavage, Conditional binding, Contact sites, Cordingley, Dexamethasone, Dnaase, Dnaase site, Dnaase sites, Enhancer, Exclusive binding, Experimental procedures, Footprint, Footprint pattern, Footprinting, Genomic, Glucocorticoid, Glucocorticoid receptor, Glucocorticoid treatment, Grange, Grus, Hager, Hepatoma, Hepatoma cell, Hepatoma cells, Hnf5, Hnf5 binding, Hnfs, Hyperreactive, Hyperreactive bands, Lmpcr, Lmpcr products, Lower strand, Methylation, Methylation interference analysis, Mmtv, Mmtv promoter, Nuclear factors, Nucleosomal structure, Nucleosome, Nucleosomes, Nucleotide sequence, Oligonucleotide, Other proteins, Permeabilized, Permeabilized cells, Primer, Promoter, Receptor, Right hand side, Schlitz, Schmid, Steroid, Transcription, Transcription factors, Transcriptional, Tumor virus, Tyrosine aminotransferase, Upper strand, Vivo, Vivo dnaase, Vivo footprinting.
Abstract
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.
Url:
DOI: 10.1016/0092-8674(91)90370-E
Affiliations:
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<term>Binding site</term>
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<term>Chromatin</term>
<term>Chromatin structure</term>
<term>Cleavage</term>
<term>Conditional binding</term>
<term>Contact sites</term>
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<term>Dexamethasone</term>
<term>Dnaase</term>
<term>Dnaase site</term>
<term>Dnaase sites</term>
<term>Enhancer</term>
<term>Exclusive binding</term>
<term>Experimental procedures</term>
<term>Footprint</term>
<term>Footprint pattern</term>
<term>Footprinting</term>
<term>Genomic</term>
<term>Glucocorticoid</term>
<term>Glucocorticoid receptor</term>
<term>Glucocorticoid treatment</term>
<term>Grange</term>
<term>Grus</term>
<term>Hager</term>
<term>Hepatoma</term>
<term>Hepatoma cell</term>
<term>Hepatoma cells</term>
<term>Hnf5</term>
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<term>Hyperreactive</term>
<term>Hyperreactive bands</term>
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<term>Methylation</term>
<term>Methylation interference analysis</term>
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<term>Nucleosomal structure</term>
<term>Nucleosome</term>
<term>Nucleosomes</term>
<term>Nucleotide sequence</term>
<term>Oligonucleotide</term>
<term>Other proteins</term>
<term>Permeabilized</term>
<term>Permeabilized cells</term>
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<term>Schmid</term>
<term>Steroid</term>
<term>Transcription</term>
<term>Transcription factors</term>
<term>Transcriptional</term>
<term>Tumor virus</term>
<term>Tyrosine aminotransferase</term>
<term>Upper strand</term>
<term>Vivo</term>
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<term>Vivo footprinting</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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