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NC2α Interacts with BTAF1 and Stimulates Its ATP-Dependent Association with TATA-Binding Protein

机译:NC2α与BTAF1相互作用并刺激其与TATA结合蛋白的ATP依赖性结合

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Transcriptional activity of the TATA-binding protein (TBP) is controlled by a variety of proteins. The BTAF1 protein (formerly known as TAFII170/TAF-172 and the human ortholog of Saccharomyces cerevisiae Mot1p) and the NC2 complex composed of NC2α (DRAP1) and NC2β (Dr1) are able to bind to TBP directly and regulate RNA polymerase II transcription both positively and negatively. Here, we present evidence that the NC2α subunit interacts with BTAF1. In contrast, the NC2β subunit is not able to associate with BTAF1 and seems to interfere with the BTAF1-TBP interaction. Addition of NC2α or the NC2 complex can stimulate the ability of BTAF1 to interact with TBP. This function is dependent on the presence of ATP in cell extracts but does not involve the ATPase activity of BTAF1 nor phosphorylation of NC2α. Together, our results constitute the first evidence of the physical cooperation between BTAF1 and NC2α in TBP regulation and provide a framework to understand transcription functions of NC2α and NC2β in vivo.
机译:TATA结合蛋白(TBP)的转录活性受多种蛋白控制。 BTAF1蛋白(以前称为TAF II 170 / TAF-172和人类酿酒酵母Mot1p的人类直系同源物)以及由NC2α(DRAP1)和NC2β( Dr1)能够直接与TBP结合并能正向和负向调节RNA聚合酶II的转录。在这里,我们提供了NC2α亚基与BTAF1相互作用的证据。相反,NC2β亚基不能与BTAF1缔合,似乎会干扰BTAF1-TBP相互作用。添加NC2α或NC2复合物可以刺激BTAF1与TBP相互作用的能力。此功能取决于细胞提取物中ATP的存在,但不涉及BTAF1的ATPase活性或NC2α的磷酸化。在一起,我们的结果构成了TBAF调节中BTAF1和NC2α之间的物理合作的第一个证据,并提供了一个了解NC2α和NC2β在体内转录功能的框架。

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