Cooperativity in transactivation between retinoic acid receptor and TFIID requires an activity analogous to E1A

Cell. 1992 May 1;69(3):401-12. doi: 10.1016/0092-8674(92)90443-g.

Abstract

In embryonal carcinoma (EC) cells retinoic acid (RA) strongly induces transcription from the RA receptor beta 2 (RAR beta 2) promoter through an RA response element (RARE) located in close proximity to the TATA box. Here we demonstrate that recombinant human TATA box-binding protein, hTFIID, and RAR functionally cooperate in transactivation of the RAR beta 2 promoter in EC cells in a strictly RA-dependent manner. We demonstrate that the core domain of hTFIID is sufficient to mediate RAR-dependent transcription and that Drosophila, but not yeast, TFIID can substitute for hTFIID. In COS cells ectopic expression of the E1A protein is a prerequisite for hTFIID and RAR to cooperate in transactivation. We propose a model for transcriptional regulation of the RAR beta 2 promoter in EC cells in which RAR, following activation by RA, functionally interacts with hTFIID via an E1A-like activity present in EC cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenovirus Early Proteins
  • Animals
  • Base Sequence
  • Binding Sites
  • Carrier Proteins / physiology*
  • Cell Line
  • Chlorocebus aethiops
  • DNA Mutational Analysis
  • Drosophila melanogaster / physiology
  • Gene Expression Regulation
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • Oncogene Proteins, Viral / physiology
  • Promoter Regions, Genetic
  • Receptors, Retinoic Acid
  • Regulatory Sequences, Nucleic Acid
  • Saccharomyces cerevisiae
  • Species Specificity
  • Transcription Factor TFIID
  • Transcription Factors / physiology*
  • Transcriptional Activation*

Substances

  • Adenovirus Early Proteins
  • Carrier Proteins
  • Oncogene Proteins, Viral
  • Receptors, Retinoic Acid
  • Transcription Factor TFIID
  • Transcription Factors