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

被引:130
作者
McEwan, IJ [1 ]
Gustafsson, JA [1 ]
机构
[1] KAROLINSKA INST, NOVUM, DEPT BIOSCI, S-14157 HUDDINGE, SWEDEN
关键词
D O I
10.1073/pnas.94.16.8485
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 AR(142-485) 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 AR(142-485). Taken together these results suggest that one mechanism of transcriptional activation by the AR involves binding to TFIIF and recruitment of the transcriptional machinery.
引用
收藏
页码:8485 / 8490
页数:6
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