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Reversible activation of non-steroid binding oestrogen receptor

Academic Article
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Overview

authors

  • Raymoure, W. J.
  • McNaught, R. W.
  • Smith, Roy

publication date

  • 1985

journal

  • Nature  Journal

abstract

  • Two high-affinity oestrogen receptors have been identified in the chick oviduct with equilibrium dissociation constants (Kd) of 0.1 and 1 nM, differing in their binding kinetics, role in ovalbumin synthesis and independent regulation in vivo. The higher-affinity receptor (X) increases RNA polymerase II activity directly, whereas the low-affinity receptor (Y) seems to be necessary to confer specificity to transcription of oestrogen-dependent genes. Acute administration of progesterone to oestrogen-stimulated chicks results in preferential destruction of the nuclear Y receptor accompanied by interruption of ovalbumin gene transcription. Here we demonstrate that receptor Y exists in a non-oestradiol binding form (Ynb) which can be activated to the binding form in vitro by treatment with either ATP or ADP. Furthermore, dialysis of oviduct cytosol, which has no effect on the high-affinity receptor X, converts receptor Y to Ynb; receptor Y can then be recovered by treatment with ATP in the presence of Mg2+ and independently of Ca2+. This is the first report of the controlled interconversion between a non-steroid binding form of oestrogen receptor and active receptor in a tissue that contains two independently regulated oestrogen receptor types.

subject areas

  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Allosteric Regulation
  • Animals
  • Chickens
  • Cytosol
  • Estradiol
  • Female
  • Guanosine Triphosphate
  • Oviducts
  • Receptors, Estrogen
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Identity

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/314745a0

PubMed ID

  • 3990803
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Additional Document Info

start page

  • 745

end page

  • 747

volume

  • 314

issue

  • 6013

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