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Potential RNA polymerase II-induced interactions of transcription factor TFIIB.

机译：潜在的RNA聚合酶II诱导的转录因子TFIIB的相互作用。

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The ubiquitous transcription factor TFIIB is required for initiation by RNA polymerase II and serves as a target of some regulatory factors. The carboxy-terminal portion of TFIIB contains a large imperfect direct repeat reminiscent of the structural organization of the TATA-binding component (TBP) of TFIID, as well as sequence homology to conserved regions of bacterial sigma factors. The present study shows that the carboxy-terminal portion of TFIIB, like that of TBP, is folded into a compact protease-resistant core. The TFIIB core, unlike the TBP core, is inactive in transcription but retains structural features that enable it to form a complex with promoter-bound TFIID. The protease-susceptible amino terminus appears to contain components responsible for direct interaction with RNA polymerase II (in association with TFIIF) either on the promoter (in association with TFIID) or independently. In addition, core TFIIB (but not intact TFIIB) extends the footprint of TBP on promoter DNA, suggesting that TFIIB has a cryptic DNA-binding potential. These results are consistent with a model in which TFIIB, in a manner functionally analogous to that of bacterial sigma factors, undergoes an RNA polymerase II-dependent conformational change with resultant DNA interactions during the pathway leading to a functional preinitiation complex.
机译：RNA聚合酶II启动需要普遍存在的转录因子TFIIB，并且它是某些调节因子的靶标。 TFIIB的羧基末端部分包含一个很大的不完善的直接重复序列，让人联想到TFIID的TATA结合成分（TBP）的结构组织，以及与细菌sigma因子保守区的序列同源性。本研究表明，TFIBB的羧基末端部分与TBP一样，被折叠成一个紧密的蛋白酶抗性核心。与TBP核心不同，TFIIB核心在转录中是无活性的，但保留了使其能够与启动子结合的TFIID形成复合物的结构特征。蛋白酶敏感的氨基末端似乎含有在启动子上（与TFIID结合）或独立与RNA聚合酶II（与TFIIF结合）直接相互作用的成分。此外，核心TFIIB（而不是完整的TFIIB）扩大了TBP在启动子DNA上的覆盖范围，这表明TFIIB具有潜在的DNA结合潜力。这些结果与模型相符，在该模型中，TFIIB以与细菌sigma因子的功能类似的方式，经历了RNA聚合酶II依赖性构象变化，并在导致功能性预起始复合物的途径中发生了DNA相互作用。

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