The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein
The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein
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DOI：
10.1128/mcb.18.2.1003
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发表时间：
1998-02-01
影响因子：
5.3
通讯作者：
Nakatani, Y
中科院分区：
文献类型：
--
作者：
Kokubo, T;Swanson, MJ;Nakatani, Y
果蝇230 kDa TfiID亚基（DTAF230）与存在于同一复合物中的TATA盒结合蛋白（TBP）的DNA结合结构域相互作用。在这里，我们表征了与DTAF230同源的酵母TAF145（YTAF145）中的抑制域。突变研究表明，N末端抑制区（残基10至71）可以分为两个亚域，I（残基10至37）和LI（残基36至71）。任何一个亚域中的突变都显着损害了功能。亚域II中的酸性残基对于与TBP的相互作用很重要。另外，通过突变TBP凸表面上的基本残基，这对于与TFIIA相互作用至关重要，从而损害了YTAF145相互作用。始终如一，TFIIA和YTAF145在竞争性TBP方面进行了竞争。 YTAF145抑制域的缺失导致温度敏感的生长表型。重要的是，TFIIA亚基的过表达抑制了这种表型，表明YTAF145抑制域参与TFIIA功能。
The Drosophila 230-kDa TFIID subunit (dTAF230) interacts with the DNA binding domain of TATA box-binding protein (TBP) which exists in the same complex. Here, we characterize the inhibitory domain in the yeast TAF145 (yTAF145), which is homologous to dTAF230. Mutation studies show that the N-terminal inhibitory region (residues 10 to 71) can be divided into two subdomains, I (residues 10 to 37) and LI (residues 36 to 71). Mutations in either subdomain significantly impair function. Acidic residues in subdomain II are important for the interaction with TBP. In addition, yTAF145 interaction is impaired by mutating the basic residues on the convex surface of TBP, which are crucial for interaction with TFIIA. Consistently, TFIIA and yTAF145 hind competitively to TBP. A deletion of the inhibitory domain of yTAF145 leads to a temperature-sensitive growth phenotype. Importantly, this phenotype is suppressed by overexpression of the TFIIA subunits, indicating that the yTAF145 inhibitory domain is involved in TFIIA function.