Tansey W P, Herr W
Cold Spring Harbor Laboratory, 1 Bungtown Road, Post Office Box 100, Cold Spring Harbor, NY 11724, USA.
Science. 1997 Feb 7;275(5301):829-31. doi: 10.1126/science.275.5301.829.
Interaction between the TATA box-binding protein TBP and TFIIB is critical for transcription in vitro. An altered-specificity TBP-TFIIB interaction was rationally designed and linked in sequence to an altered-specificity TATA box-TBP interaction to study how TBP and TFIIB function together to support transcription in human cells. The activity of this altered-specificity TATA-TBP-TFIIB array demonstrated that many activators use the known TBP-TFIIB interaction to stimulate transcription. One activator, however, derived from a glutamine-rich activation domain of Sp1, activated transcription independently of this interaction. These results reveal that selectivity in activator function in vivo can be achieved through differential use of TBP and TFIIB.
TATA 盒结合蛋白 TBP 与 TFIIB 之间的相互作用对于体外转录至关重要。合理设计了一种特异性改变的 TBP-TFIIB 相互作用,并在序列上与特异性改变的 TATA 盒-TBP 相互作用相连接,以研究 TBP 和 TFIIB 如何共同发挥作用来支持人类细胞中的转录。这种特异性改变的 TATA-TBP-TFIIB 阵列的活性表明,许多激活剂利用已知的 TBP-TFIIB 相互作用来刺激转录。然而,一种源自 Sp1 富含谷氨酰胺激活结构域的激活剂,独立于这种相互作用激活转录。这些结果表明,体内激活剂功能的选择性可以通过对 TBP 和 TFIIB 的不同利用来实现。