Cell
Volume 55, Issue 1, 7 October 1988, Pages 145-156
Journal home page for Cell

Article
The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer

https://doi.org/10.1016/0092-8674(88)90017-7Get rights and content

Abstract

Extracts containing wild-type or mutant human estrogen receptor (ER) have been used to study the binding of ER to its responsive element (ERE). Estradiol (E2) or the antiestrogen hydroxytamoxifen is required for ER binding as assayed by gel retardation. The DNA binding domain (DBD) encompasses the highly conserved region C. Both intact ER-E2 complexes and ER mutants truncated for the hormone binding domain (HBD) bind as dimers to an ERE. However, an HBD-truncated ER binds less tightly to an ERE than an intact ER-E2 complex. The DBD and the HBD contain a constitutive and a stronger ER-induced dimerization function, respectively. Thus, in addition to inducing the activation function associated with the HBD, estrogen plays a crucial role in the formation of stable ER dimers that bind tightly to ERE.

References (52)

  • C. Lee et al.

    Copper staining: a five-minute protein stain for sodium dodecyl sulfate-polyacrylamide gels

    Anal. Biochem.

    (1987)
  • A.D. Linstedt et al.

    Analysis of monomeric-dimeric states of the estrogen receptor with monoclonal antiestrophilins

    J. Steroid Biochem.

    (1986)
  • A. Maxam et al.

    Sequencing end-labeled DNA with base-specific chemical cleavages

    Meth. Ezymol.

    (1980)
  • W.B. Pratt et al.

    A region in the steroid binding domain determines formation of the non-DNA-binding, 9S glucocorticoid receptor complex

    J. Biol. Chem.

    (1988)
  • N.J.G. Webster et al.

    The yeast UASG is a transcriptional enhancer in human HeLa cells in the presence of the GAL4 trans-activator

    Cell

    (1988)
  • N.J.G. Webster et al.

    The hormone-binding domains of the estrogen and glucocorticoid receptors contain an inducible transcription activation function

    Cell

    (1988)
  • J.M. Berg

    More metal-binding fingers

    Nature

    (1986)
  • R. Breathnach et al.

    Plasmids for the cloning and expression of full-length double-stranded cDNAs under control of the SV40 early or late gene promoter

    Nucl. Acids Res.

    (1983)
  • L.A. Chodosh et al.

    A single polypeptide possesses the binding and transcription activities of the adenovirus major late transcription factor

    Mol. Cell. Biol.

    (1986)
  • M. Denis et al.

    Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state

    Nature

    (1988)
  • R.M. Evans

    The steroid and thyroid hormone receptor superfamily

    Science

    (1988)
  • P.J. Godowski et al.

    Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement

    Nature

    (1987)
  • S. Green et al.

    A superfamily of potentially oncogenic hormone receptors

    Nature

    (1986)
  • S. Green et al.

    Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor

    Nature

    (1987)
  • S. Green et al.

    Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A

    Nature

    (1986)
  • S. Green et al.

    The N-terminal DNA-binding “zinc-finger” of the oestrogen and glucocorticoid receptors determines target gene specificity

    EMBO J.

    (1988)
  • Cited by (0)

    View full text