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.
Mesh Terms:
DNA-Binding Proteins, Escherichia coli, Humans, Male, Receptors, Androgen, Recombinant Proteins, Transcription Factors, Transcription Factors, TFII, Transcriptional Activation
Proc. Natl. Acad. Sci. U.S.A.
Date: Aug. 05, 1997
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