INTERACTION BETWEEN THE N-TERMINAL DOMAIN OF THE 230-KDA SUBUNIT AND THE TATA BOX-BINDING SUBUNIT OF TFIID NEGATIVELY REGULATES TATA-BOX BINDING
INTERACTION BETWEEN THE N-TERMINAL DOMAIN OF THE 230-KDA SUBUNIT AND THE TATA BOX-BINDING SUBUNIT OF TFIID NEGATIVELY REGULATES TATA-BOX BINDING
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DOI：
10.1073/pnas.91.9.3520
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发表时间：
1994-04-26
影响因子：
11.1
通讯作者：
NAKATANI, Y
中科院分区：
文献类型：
--
作者：
KOKUBO, T;YAMASHITA, S;NAKATANI, Y
转录起始因子TFIID在转录调控中发挥核心作用。果蝇TFIID是一种由TATA盒结合多肽(TBP)和一些紧密结合的多肽组成的多聚体蛋白。以前，TFIID最大的提交序列(P230)被克隆并证明在没有其他亚基的情况下抑制TBP的TATA盒结合。在这里，我们证明了P230至少包含两个与TBP相互作用的位点，并且N-末端既介导了与TBP的强烈物理相互作用，也介导了TBP功能的抑制。详细的突变研究表明，抑制区和强TBP结合区无法区分，从而表明P230N末端区域与TBP的相互作用可能直接控制TATA盒的结合。
Transcription initiation factor TFIID plays a central role in transcriptional regulation. Drosophila TFIID is a multimeric protein consisting of the TATA box-binding polypeptide (TBP) and a number of tightly associated polypeptides. Previously, the largest submit of TFIID (p230) was cloned and demonstrated to inhibit the TATA-box binding of TBP in the absence of other subunits. Here we demonstrate that p230 contains at least two sites of interaction with TBP and that the N-terminal site mediates both strong physical interactions with TBP and inhibition of the TBP function. A detailed mutagenesis study shows that the inhibitory domain is indistinguishable from the strong TBP-binding domain, thus indicating that interaction of the p230 N-terminal region with TBP may directly control TATA-box binding.