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The human estrogen receptor has two independent nonacidic transcriptional activation functions

Identifieur interne : 000397 ( France/Analysis ); précédent : 000396; suivant : 000398

The human estrogen receptor has two independent nonacidic transcriptional activation functions

Auteurs : Laszio Tora [France] ; John White [France] ; Christel Brou [France] ; Dlane Tasset [France] ; Nicholas Webster [France] ; Elisabeth Scheer [France] ; Plerre Chambon [France]

Source :

RBID : ISTEX:B1C9A6CA16A0FDB9DD843EF64E0AEA58F3737564

English descriptors

Abstract

Abstract: We have previously reported the presence of a hormone-Inducible transcriptional activation function (TAF-2) within the region of the estrogen receptor (ER) that contains the hormone binding domain. We show here that the N-terminal A B region of the ER contains an Independent constitutive activation function (TAF-1) that exhibits cell type specificity since it activates transcription efficiently in chicken embryo fibroblasts, but only poorly in HeLa cells. By analyzing the ability of TAF-1, TAF-2, and the GAL4 and VP16 acidic activating domains (AADs) to homosynergize and heterosynergize with one another and with the factor binding to the upstream element (UE) of the adenovirus 2 major late promoter, we show that the activation properties of TAF-1 and TAF-2 are different and distinct from those of AADs, in agreement with the absence of acidic amino acid stretches in TAF-1 and TAF-2.

Url:
DOI: 10.1016/0092-8674(89)90031-7


Affiliations:


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ISTEX:B1C9A6CA16A0FDB9DD843EF64E0AEA58F3737564

Le document en format XML

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<term>Aads</term>
<term>Acidic</term>
<term>Acidic activators</term>
<term>Activates transcription</term>
<term>Activation</term>
<term>Activation function</term>
<term>Activation functions</term>
<term>Activator</term>
<term>Activator expression vectors</term>
<term>Additive effects</term>
<term>Amino</term>
<term>Amino acids</term>
<term>Assay</term>
<term>Cell types</term>
<term>Chambon</term>
<term>Chicken embryo fibroblasts</term>
<term>Chimeric</term>
<term>Chimeric activators</term>
<term>Densitometric scanning</term>
<term>Embo</term>
<term>Embryo</term>
<term>Enhancer</term>
<term>Estrogen</term>
<term>Estrogen receptor</term>
<term>Experimental procedures</term>
<term>Expression vectors</term>
<term>Gal4</term>
<term>Glucocorticoid receptors</term>
<term>Hela</term>
<term>Hela cells</term>
<term>Heterosynergize</term>
<term>Homosynergism</term>
<term>Human estrogen receptor</term>
<term>Independent transfections</term>
<term>Internal control</term>
<term>Kumar</term>
<term>Minimal promoter</term>
<term>Minimal promoters</term>
<term>More transcription</term>
<term>Mpmlp</term>
<term>Nuclear receptors</term>
<term>Nuclease</term>
<term>Nuclease analyses</term>
<term>Nuclease analysis</term>
<term>Oestrogen</term>
<term>Petri dishes</term>
<term>Plasmid</term>
<term>Promoter</term>
<term>Ptashne</term>
<term>Receptor</term>
<term>Reporter gene</term>
<term>Reporter genes</term>
<term>Reporter plasmids</term>
<term>Synergistically</term>
<term>Synergize</term>
<term>Tata</term>
<term>Tata region</term>
<term>Tora</term>
<term>Transcription</term>
<term>Transcription factor</term>
<term>Transcriptional</term>
<term>Transfected</term>
<term>Transfections</term>
<term>Unpublished data</term>
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<div type="abstract" xml:lang="en">Abstract: We have previously reported the presence of a hormone-Inducible transcriptional activation function (TAF-2) within the region of the estrogen receptor (ER) that contains the hormone binding domain. We show here that the N-terminal A B region of the ER contains an Independent constitutive activation function (TAF-1) that exhibits cell type specificity since it activates transcription efficiently in chicken embryo fibroblasts, but only poorly in HeLa cells. By analyzing the ability of TAF-1, TAF-2, and the GAL4 and VP16 acidic activating domains (AADs) to homosynergize and heterosynergize with one another and with the factor binding to the upstream element (UE) of the adenovirus 2 major late promoter, we show that the activation properties of TAF-1 and TAF-2 are different and distinct from those of AADs, in agreement with the absence of acidic amino acid stretches in TAF-1 and TAF-2.</div>
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