Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF

Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8485-90. doi: 10.1073/pnas.94.16.8485.

Abstract

The human androgen receptor (AR) is a ligand-activated transcription factor that regulates genes important for male sexual differentiation and development. To better understand the role of the receptor as a transcription factor we have studied the mechanism of action of the N-terminal transactivation function. In a protein-protein interaction assay the AR N terminus (amino acids 142-485) selectively bound to the basal transcription factors TFIIF and the TATA-box-binding protein (TBP). Reconstitution of the transactivation activity in vitro revealed that AR142-485 fused to the LexA protein DNA-binding domain was competent to activate a reporter gene in the presence of a competing DNA template lacking LexA binding sites. Furthermore, consistent with direct interaction with basal transcription factors, addition of recombinant TFIIF relieved squelching of basal transcription by AR142-485. Taken together these results suggest that one mechanism of transcriptional activation by the AR involves binding to TFIIF and recruitment of the transcriptional machinery.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Escherichia coli
  • Humans
  • Male
  • Receptors, Androgen / genetics*
  • Receptors, Androgen / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism
  • Transcription Factors, TFII*
  • Transcriptional Activation*

Substances

  • DNA-Binding Proteins
  • Receptors, Androgen
  • Recombinant Proteins
  • Transcription Factors
  • Transcription Factors, TFII
  • transcription factor TFIIF