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首页> 外文期刊>Molecular and Cellular Biology >A highly conserved domain of RNA polymerase II shares a functional element with acidic activation domains of upstream transcription factors.
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A highly conserved domain of RNA polymerase II shares a functional element with acidic activation domains of upstream transcription factors.

机译：RNA聚合酶II的高度保守的结构域与上游转录因子的酸性激活结构域共享功能元件。

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摘要

We report here that the largest subunit of yeast RNA polymerase II contains an acidic domain that is similar to acidic activators of transcription. This domain includes the highly conserved homology box H. A hybrid protein containing this acidic domain fused to the DNA-binding domain of GAL4 is a potent activator of transcription in the yeast Saccharomyces cerevisiae. Interestingly, mutations that reduce the upstream activating activity of this acidic domain also abolish the normal function of RNA polymerase II. Such functional defects can be rescued by the acidic activation domains of VP16 and GAL4 when inserted into the mutant derivatives of RNA polymerase II. We further show that this acidic domain of RNA polymerase II interacts directly with two general transcription factors, the TATA-binding protein and TFIIB, and that the acidic activation domain of VP16 can compete specifically with the acidic domain of the RNA polymerase for these interactions. We discuss the implications of this finding for the mechanisms of transcriptional activation in eucaryotes.
机译：我们在这里报告，酵母RNA聚合酶II的最大亚基包含一个酸性域，类似于转录的酸性激活剂。该结构域包括高度保守的同源框H。含有该酸性结构域与GAL4的DNA结合结构域融合的杂合蛋白是酿酒酵母中一种有效的转录激活因子。有趣的是，降低该酸性结构域上游激活活性的突变也消除了RNA聚合酶II的正常功能。当插入到RNA聚合酶II的突变衍生物中时，可以通过VP16和GAL4的酸性激活域来挽救这种功能缺陷。我们进一步表明，这种RNA聚合酶II的酸性结构域与两个通用转录因子TATA结合蛋白和TFIIB直接相互作用，并且VP16的酸性激活结构域可以与RNA聚合酶的酸性域竞争这些相互作用。我们讨论了这一发现对真核生物转录激活机制的影响。

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