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首页> 外文期刊>Nature >Connecting a promoter-bound protein to TBP bypasses the need for a transcriptional activation domain.
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Connecting a promoter-bound protein to TBP bypasses the need for a transcriptional activation domain.

机译：将与启动子结合的蛋白连接至TBP绕过了对转录激活域的需求。

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摘要

Biochemical analyses have suggested potential targets for transcriptional activation domains, which include several components of the RNA polymerase II machinery, as well as the chromatin template. Here we examine the mechanism of transcriptional activation in yeast cells by connecting a heterologous DNA-binding domain (LexA) to the TATA-binding protein (TBP). LexA-TBP efficiently activates transcription from a promoter containing a LexA operator upstream of a TATA element. Activation is promoter-specific and is sensitive to mutations on the DNA-binding surface of TBP; hence it is not due to a fortuitous activation domain on TBP. Thus a promoter-bound protein lacking an activation domain can stimulate transcription if it is directly connected to TBP. This suggests that recruitment of TBP to the promoter can be a rate-limiting step for transcription in vivo, and that interactions between activation domains and factors that function after TBP recruitment can be bypassed for activation.
机译：生化分析已为转录激活域建议了潜在的靶标，其中包括RNA聚合酶II机器的几种成分以及染色质模板。在这里，我们通过将异源DNA结合域（LexA）连接到TATA结合蛋白（TBP），来检查酵母细胞中转录激活的机制。 LexA-TBP有效激活来自TATA元件上游包含LexA操纵子的启动子的转录。激活是启动子特异性的，并且对TBP DNA结合表面的突变敏感。因此，这不是由于TBP上的偶然激活域引起的。因此，如果缺乏激活域的启动子结合蛋白直接与TBP连接，则可以刺激转录。这表明将TBP募集到启动子可以是体内转录的限速步骤，并且可以绕过激活域和TBP募集后起作用的因子之间的相互作用进行激活。

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