Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.
Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.
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DOI：
10.7554/elife.30395
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发表时间：
2017-11-07
期刊：
影响因子：
7.7
通讯作者：
Berger I
中科院分区：
文献类型：
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作者：
Gupta K;Watson AA;Baptista T;Scheer E;Chambers AL;Koehler C;Zou J;Obong-Ebong I;Kandiah E;Temblador A;Round A;Forest E;Man P;Bieniossek C;Laue ED;Lemke EA;Rappsilber J;Robinson CV;Devys D;Tora L;Berger I
一般转录因子TFIID是RNA聚合酶II转录起始的关键组分。人TFIID是由TBP结合蛋白（TBP）和13个TBP相关因子（TAFs）组成的巨噬子复合物。TBP与核心启动子DNA结合，识别TATA-box。我们发现了一个由TBP和包含TFIID亚基TAF11和TAF13的组蛋白折叠（HF）结构域形成的三元复合物。我们证明了TAF11/TAF13与TATA-box DNA的TBP结合竞争，也与之前涉及TATA-box模仿的TAF1的n端结构域竞争。通过结合晶体坐标、生化分析和交联质谱（CLMS）数据的综合方法，我们确定了TAF11/TAF13/TBP复合物的结构，揭示了TAF11/TAF13与TBP DNA结合表面的相互作用。我们在TAF13中发现了一个高度保守的c端tbp相互作用结构域（CTID），这对支持细胞生长至关重要。因此，我们的研究结果对细胞TFIID组装有影响，并提出了一种新的TFIID功能调节状态。
General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain-containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function.