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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Structural insights of HutP-mediated regulation of transcription of the hut operon in Bacillus subtilis.
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Structural insights of HutP-mediated regulation of transcription of the hut operon in Bacillus subtilis.

机译：HutP介导的枯草芽孢杆菌小屋操纵子转录调控的结构见解。

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摘要

Regulating gene expression directly at the mRNA level represents a novel approach to control cellular processes in all organisms. In this respect, an RNA-binding protein plays a key role by targeting the mRNA to regulate the expression by attenuation or an anti-termination mechanism only in the presence of their cognate ligands. Although many proteins are known to use these mechanisms to regulate the gene expression, no structural insights have been revealed to date to explain how these proteins trigger the conformation for the recognition of RNA. This review describes the activated conformation of HutP, brought by the coordination of L-histidine and Mg(2+) ions, based on our recently solved crystal structures [uncomplexed HutP, HutP-Mg(2+), HutP-L-histidine, HutP-Mg(2+)-L-histidine, HutP-Mg(2+)-L-histidine-RNA]. Once the HutP is activated, the protein binds specifically to bases within the terminator region, without undergoing further structural rearrangement. Also, a high resolution (1.48 A) crystal structure of the quaternary complex containing the three GAG motifs is presented. This analysis clearly demonstrates that the first base in the UAG motifs is not important for the function and is consistent with our previous observations.
机译：直接在mRNA水平上调节基因表达代表了一种控制所有生物中细胞过程的新颖方法。在这方面，RNA结合蛋白仅在它们的同源配体存在时，通过靶向mRNA以通过减毒或抗终止机制调节表达来发挥关键作用。尽管已知许多蛋白质使用这些机制来调节基因表达，但迄今为止，尚未发现任何结构性见解来解释这些蛋白质如何触发构象以识别RNA。这篇评论根据我们最近解决的晶体结构[未复合的HutP，HutP-Mg（2 +），HutP-L-组氨酸， HutP-Mg（2 +）-L-组氨酸，HutP-Mg（2 +）-L-组氨酸-RNA]。一旦激活了HutP，该蛋白质即可与终止子区域内的碱基特异性结合，而无需进行进一步的结构重排。此外，提出了包含三个GAG图案的四元络合物的高分辨率（1.48 A）晶体结构。该分析清楚地表明，UAG基序中的第一个碱基对该功能并不重要，并且与我们先前的观察结果一致。

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