The TBP-TFIIA interaction in the response to acidic activators in vivo.
The TBP-TFIIA interaction in the response to acidic activators in vivo.
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TBP-TFIIA 相互作用对体内酸性激活剂的反应。
DOI：
10.1126/science.7604282
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Struhl,K
中科院分区：
文献类型：
--
作者：
Stargell,LA;Struhl,K
本文描述了一种酵母TBP突变体（N2-1），其在体内对酸性活化剂的特异性应答中有缺陷。N2-1不支持Gal 4、Ace 1和Gcn 4的激活，但对于组成型转录、Cyc 8-Tup 1和Not复合物的抑制以及聚合酶I（Pol）和Pol III的转录似乎不受影响。在体外，N2-1不能与TFIIA相互作用，但它通常与TATA元件、酸性活化结构域和TFIIB相关联。TFIIA的小亚基与N2-1的融合在体内恢复激活功能。因此，TBP和TFIIA之间的有效相互作用是体内转录激活所必需的。
A yeast TBP mutant (N2-1) is described here that is defective specifically in responding to acidic activators in vivo. N2-1 does not support activation by Gal4, Ace1, and Gcn4, but appears unaffected for constitutive transcription, repression by the Cyc8-Tup1 and Not complexes, and transcription by polymerase I (Pol) and Pol III. In vitro, N2-1 fails to interact with TFIIA, but it associates normally with a TATA element, an acidic activation domain, and TFIIB. Fusion of the small subunit of TFIIA to N2-1 restores activation function in vivo. Thus, an efficient interaction between TBP and TFIIA is required for transcriptional activation in vivo.