Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF.
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.
McEwan
I J
IJ
Department of Biosciences, Novum, Karolinska Institute, S-141 57 Huddinge, Sweden. iain.mcewan@abdn.ac.uk
Gustafsson
J
J
D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli; D006801:Humans; D008297:Male; D011944:Receptors, Androgen / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism; D019473:Transcription Factors, TFII; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; D011944:Receptors, Androgen; D011994:Recombinant Proteins; D014157:Transcription Factors; D019473:Transcription Factors, TFII; C056604:transcription factor TFIIF