The human estrogen receptor has two independent nonacidic transcriptional activation functions

Cell. 1989 Nov 3;59(3):477-87. doi: 10.1016/0092-8674(89)90031-7.


We have previously reported the presence of a hormone-inducible transcriptional activation function (TAF-2) within the region of the estrogen receptor (ER) that contains the hormone binding domain. We show here that the N-terminal A/B region of the ER contains an independent constitutive activation function (TAF-1) that exhibits cell type specificity since it activates transcription efficiently in chicken embryo fibroblasts, but only poorly in HeLa cells. By analyzing the ability of TAF-1, TAF-2, and the GAL4 and VP16 acidic activating domains (AADs) to homosynergize and heterosynergize with one another and with the factor binding to the upstream element (UE) of the adenovirus 2 major late promoter, we show that the activation properties of TAF-1 and TAF-2 are different and distinct from those of AADs, in agreement with the absence of acidic amino acid stretches in TAF-1 and TAF-2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Chick Embryo
  • Chimera
  • Enhancer Elements, Genetic*
  • Fibroblasts / metabolism
  • Gene Expression Regulation*
  • HeLa Cells / metabolism
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Oligonucleotide Probes
  • Plasmids
  • Receptors, Estrogen / genetics
  • Receptors, Estrogen / metabolism*
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*
  • Transcription, Genetic
  • Transfection


  • Oligonucleotide Probes
  • Receptors, Estrogen
  • Trans-Activators