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Titolo:
Estrogen response element binding induces alterations in estrogen receptor-alpha conformation as revealed by susceptibility to partial proteolysis
Autore:
Ramsey, TL; Klinge, CM;
Indirizzi:
Univ Louisville, Sch Med, Dept Biochem & Mol Biol, Louisville, KY 40292 USA Univ Louisville Louisville KY USA 40292 ol Biol, Louisville, KY 40292 USA
Titolo Testata:
JOURNAL OF MOLECULAR ENDOCRINOLOGY
fascicolo: 3, volume: 27, anno: 2001,
pagine: 275 - 292
SICI:
0952-5041(200112)27:3<275:EREBIA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBOXYL-TERMINAL REGIONS; ACTIVATION FUNCTION AF-2; HIGH-AFFINITY BINDING; DNA IN-VITRO; LIGAND-BINDING; NUCLEAR RECEPTOR; FLANKING SEQUENCES; GENE-EXPRESSION; HALF-SITES; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Klinge, CM Univ Louisville, Sch Med, Dept Biochem & Mol Biol, Louisville, KY 40292 USA Univ Louisville Louisville KY USA 40292 uisville, KY 40292 USA
Citazione:
T.L. Ramsey e C.M. Klinge, "Estrogen response element binding induces alterations in estrogen receptor-alpha conformation as revealed by susceptibility to partial proteolysis", J MOL ENDOC, 27(3), 2001, pp. 275-292

Abstract

Genes whose expression is highly induced by estradiol (E-2) contain Multiple estrogen response elements (EREs) in their promoters. Previously we reported that estrogen receptor-alpha (ER alpha) binds cooperatively to and E-2synergistically activates reporter gene expression from three or four tandem copies of a consensus ERE (EREc38). Here we evaluated how ERa binding toone, two, three or four tandem copies of EREc38 affects ERa conformation as detected by altered ERa trypsin digestion patterns in Western blots. E-2-or 4-hydroxytamoxifen (4-OHT)-occupied ER alpha bound to the pS2 ERE or toa single copy of EREc38 showed enhanced susceptibility to trypsin digestion compared to E-2- or 4-OHT-ER alpha incubated with DNA lacking an ERE. ERabinding to multiple tandem copies of EREc38 further increased sensitivity to trypsin digestion. These results correlate with synergistic transcription and cooperativity of ER alpha binding to multiple tandem copies of EREc38. These observations suggest that EREc38 binding alters the overall conformation of ERa and that multiple tandem copies of EREc38 enhance these conformational changes. We hypothesize that ERE-induced alterations in ERa conformation modulate interaction with coregulatory proteins, resulting in synergistic transcriptional activation.

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Documento generato il 26/01/20 alle ore 09:44:44