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首页> 外文期刊>Molecular and Cellular Biology >A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo.
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A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo.

机译：TATA结合蛋白-TFIIB相互作用的严重缺陷不排除体内转录激活。

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In yeast cells, mutations in the TATA-binding protein (TBP) that disrupt the interaction with the TATA element or with TFIIA can selectively impair the response to acidic activator proteins. We analyzed the transcriptional properties of TBP derivatives in which residues that directly interact with TFIIB were replaced by alanines. Surprisingly, a derivative with a 50-fold defect in TBP-TFIIB-TATA complex formation in vitro (E188A) supports viability and responds efficiently to activators in vivo. The E186A derivative, which displays a 100-fold defect in TBP-TFIIB-TATA complex formation, does not support viability, yet it does respond to activators. Conversely, the L189A mutation, which has the mildest effect on the interaction with TFIIB (10-fold), can abolish transcriptional activation and cell viability when combined with mutations on the DNA-binding surface. This "synthetic lethal" effect is not observed with E188A, suggesting that the previously described role of L189 in transcriptional activation may be related to its location on the DNA-binding surface and not to its interaction with TFIIB. Finally, when using TBP mutants defective on multiple interaction surfaces, we observed synthetic lethal effects between mutations on the TFIIA and TFIIB interfaces but found that mutations implicated in association with polymerase II and TFIIF did not have significant effects in vivo. Taken together, these results argue that, unlike the TBP-TATA and TBP-TFIIA interactions, the TBP-TFIIB interaction is not generally limiting for transcriptional activation in vivo.
机译：在酵母细胞中，TATA结合蛋白（TBP）中的突变会破坏与TATA元件或TFIIA的相互作用，从而选择性地削弱对酸性激活蛋白的反应。我们分析了TBP衍生物的转录特性，其中直接与TFIIB相互作用的残基被丙氨酸取代。出人意料的是，在体外TBP-TFIIB-TATA复合物形成中具有50倍缺陷的衍生物（E188A）支持活力，并在体内对激活剂有效反应。 E186A衍生物在TBP-TFIIB-TATA复合物的形成中表现出100倍的缺陷，不支持活力，但确实对激活剂有反应。相反，当L189A突变与DNA结合表面的突变结合时，对TFIIB相互作用的影响最轻（10倍），可以消除转录激活和细胞活力。 E188A未观察到这种“合成致死”效应，表明L189在转录激活中的先前作用可能与其在DNA结合表面上的位置有关，而与它与TFIIB的相互作用无关。最后，当使用在多个相互作用表面上有缺陷的TBP突变体时，我们观察到了TFIIA和TFIIB界面上的突变之间的合成致死作用，但发现与聚合酶II和TFIIF相关的突变在体内没有明显的作用。综上所述，这些结果表明，与TBP-TATA和TBP-TFIIA相互作用不同，TBP-TFIIB相互作用通常不限制体内转录激活。

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