Rushmere N K, Parker M G, Davies P
Mol Cell Endocrinol. 1987 Jun;51(3):259-65. doi: 10.1016/0303-7207(87)90036-0.
The interaction of 5 alpha-dihydrotestosterone-receptor complexes with purified DNA fragments representing upstream, coding and intervening sequences of the prostate binding protein C3(1) gene was investigated using a DNA-cellulose competition binding assay. The partially purified androgen-receptor complexes which were used in the assay had proven DNA-binding capabilities. Two fragments were identified with relatively high affinity for androgen-receptor complexes. A 300 bp fragment extending from -220 to +80 and a 500 bp fragment derived entirely from the first intron consistently competed most effectively in the system. The presence of a high affinity site or sites in or near the promoter region of the gene is consistent with current models of transcriptional activation of hormone-responsive genes by steroid receptors. High affinity sites for steroid receptors within introns may indicate a role for receptors in regulation of transcription at other stages, or in post-transcriptional modification.
使用DNA-纤维素竞争结合试验,研究了5α-二氢睾酮-受体复合物与代表前列腺结合蛋白C3(1)基因上游、编码和间隔序列的纯化DNA片段之间的相互作用。试验中使用的部分纯化雄激素-受体复合物已证实具有DNA结合能力。鉴定出两个对雄激素-受体复合物具有相对高亲和力的片段。一个从-220延伸至+80的300 bp片段和一个完全源自第一个内含子的500 bp片段在该系统中始终表现出最有效的竞争。该基因启动子区域内或附近存在一个或多个高亲和力位点,这与目前类固醇受体对激素反应性基因转录激活的模型一致。内含子内类固醇受体的高亲和力位点可能表明受体在转录的其他阶段或转录后修饰中发挥作用。