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The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
KTH.
Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.ORCID iD: 0000-0003-1029-9969
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2001 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 276, no 49, 45939-45944 p.Article in journal (Refereed) Published
Abstract [en]

The N-terminal regions of the estrogen receptor ve (ER alpha -N) and beta (ER beta -N) were expressed and purified to homogeneity. Using NAM and circular dichroism spectroscopy, we conclude that both ER alpha -N and ER beta -N are unstructured in solution. The TATA box-binding protein (TBP) has been shown previously to interact with ERa-N in vitro and to potentiate ER-activated transcription. We used surface plasmon resonance and circular dichroism spectroscopy to confirm and further characterize the ER-N-TBP interaction. Our results show that the intrinsically unstructured ERa-N interacts with TBP, and suggest that structural changes are induced in ERa-N upon TBP interaction. Conformational changes upon target factor interaction have not previously been demonstrated for any N-terminal region of nuclear receptors. In addition, no binding of ER beta -N to TBP was detected. This difference in TBP binding could imply differential recruitment of target proteins by ERa-N and ER beta -N. The affinity of the ER alpha -N-TBP interaction was determined to be in the micromolar range (K-D = 10(-6) to 10(-5) m). Our results support models of TBP as a target protein for the N-terminal activation domain of ER alpha. Further, our results suggest that target proteins can induce and/or stabilize ordered structure in N-terminal regions of nuclear receptors upon interaction.

Place, publisher, year, edition, pages
2001. Vol. 276, no 49, 45939-45944 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:sh:diva-15837DOI: 10.1074/jbc.M107875200ISI: 000172573100062PubMedID: 11595744Scopus ID: 2-s2.0-0035824562OAI: oai:DiVA.org:sh-15837DiVA: diva2:509247
Available from: 2012-03-12 Created: 2012-03-09 Last updated: 2017-06-29Bibliographically approved

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CiteExportLink to record
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Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
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More styles
Language
  • de-DE
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