Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein.
Multiple functions of the nonconserved N-terminal domain of yeast TATA-binding protein.
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酵母 TATA 结合蛋白非保守 N 端结构域的多种功能。
DOI：
10.1093/genetics/158.1.87
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发表时间：
2001
期刊：
影响因子：
3.3
通讯作者：
Struhl,K
中科院分区：
文献类型：
--
作者：
Lee,M;Struhl,K
The TATA-binding protein (TBP) is composed of a highly conserved core domain sufficient for TATA-element binding and preinitiation complex formation as well as a highly divergent N-terminal region that is dispensable for yeast cell viability.In vitro, removal of the N-terminal region domain enhances TBP-TATA association and TBP dimerization. Here, we examine the effects of truncation of the N-terminal region in the context of yeast TBP mutants with specific defects in DNA binding and in interactions with various proteins. For a subset of mutations that disrupt DNA binding and the response to transcriptional activators, removal of the N-terminal domain rescues their transcriptional defects. By contrast, deletion of the N-terminal region is lethal in combination with mutations on a limited surface of TBP. Although this surface is important for interactions with TFIIA and Brf1, TBP interactions with these two factors do not appear to be responsible for this dependence on the N-terminal region. Our results suggest that the N-terminal region of TBP has at least two distinct functionsin vivo. It inhibits the interaction of TBP with TATA elements, and it acts positively in combination with a specific region of the TBP core domain that presumably interacts with another protein(s).
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将 TATA 结合蛋白招募到启动子：无需上游激活剂的转录激活
影响因子：
5.3
作者：
Hua Xiao;J. Friesen;John T. Lis
通讯作者：
John T. Lis
DOI：
10.1073/pnas.94.3.820
发表时间：
1997-02-04
影响因子：
11.1
作者：
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通讯作者：
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DOI：
10.1073/pnas.93.11.5208
发表时间：
1996-05-28
影响因子：
11.1
作者：
Iyer, V;Struhl, K
通讯作者：
Struhl, K
影响因子：
10.5
作者：
AUBLE, DT;HANSEN, KE;HAHN, S
通讯作者：
HAHN, S
影响因子：
11.4
作者：
LESCURE, A;LUTZ, Y;TORA, L
通讯作者：
TORA, L