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Human estrogen receptor forms multiple protein-DNA complexes.

M Brown1, P A Sharp

  • 1Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.

The Journal of Biological Chemistry
|July 5, 1990
PubMed
Summary
This summary is machine-generated.

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Human estrogen receptor produced in insect cells binds DNA. Hormone binding influences DNA interaction, with estradiol inducing a structural change not seen with tamoxifen, impacting gene activation.

Area of Science:

  • Molecular Biology
  • Endocrinology
  • Biochemistry

Background:

  • The human estrogen receptor (ER) plays a crucial role in gene regulation.
  • Understanding ER's DNA-binding properties is essential for comprehending its function.

Purpose of the Study:

  • To overproduce functional human estrogen receptor using a baculovirus expression system.
  • To investigate the hormone-dependent DNA binding of the estrogen receptor to the estrogen response element (ERE).

Main Methods:

  • Utilized a baculovirus expression system for recombinant human ER production in insect cells.
  • Performed electrophoretic mobility shift assays (EMSAs) to assess ER-ERE binding.
  • Investigated the effects of estradiol and tamoxifen on ER-ERE complex formation.

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Main Results:

  • Recombinant human ER was full-length, specifically bound estrogen, and was recognized by a monoclonal antibody.
  • ER-ERE binding occurred in the absence of Mg2+ regardless of estrogen presence.
  • In the presence of Mg2+, ER-ERE binding was hormone-dependent, enhanced by higher temperatures.
  • Both estradiol and tamoxifen stimulated ERE binding similarly.
  • Estradiol, but not tamoxifen, induced a conformational change in the ER, altering complex mobility in native gels.

Conclusions:

  • Estrogen receptor DNA binding is not absolutely hormone-dependent.
  • Estradiol induces a specific conformational change in the estrogen receptor, unlike tamoxifen.
  • These differential effects may explain distinct target gene activation by estradiol and tamoxifen.