Grabbing the message:: structural basis of mRNA 3′UTR recognition by Hrp1
Grabbing the message:: structural basis of mRNA 3′UTR recognition by Hrp1
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DOI：
10.1038/sj.emboj.7601190
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发表时间：
2006-07-12
期刊：
影响因子：
11.4
通讯作者：
Perez-Canadillas, Jose Manuel
中科院分区：
文献类型：
--
作者：
Perez-Canadillas, Jose Manuel
对新转录的mRNA的3‘-非翻译区内编码的特定信号的识别触发了一个多蛋白机器的组装，该机器修改了它的3’端。Hrp1识别这样的信号之一，即所谓的聚腺苷酸化增强元件(PEE)，促进酵母中其他聚腺苷酸化因子的招募。这种相互作用的分子基础在这里通过Hrp1和模拟PEE的寡核苷酸之间的络合物的溶液结构被揭示。六个连续的碱基(AUAUAU)被两个串联排列的RNA结合域特异性识别。蛋白质和RNA在形成复合体时都经历了显著的构象变化，伴随而来的是RNA碱基的大量表面埋藏。RNA特异性的关键方面可以通过分子间芳香接触和氢键的存在来解释。总之，Hrp1-pee结构代表了在原子水平上理解切割和聚腺苷酸化机制组装的第一步。
The recognition of specific signals encoded within the 3'-untranslated region of the newly transcribed mRNA triggers the assembly of a multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The molecular bases of this interaction are revealed here by the solution structure of a complex between Hrp1 and an oligonucleotide mimicking the PEE. Six consecutive bases (AUAUAU) are specifically recognised by two RNA-binding domains arranged in tandem. Both protein and RNA undergo significant conformational changes upon complex formation with a concomitant large surface burial of RNA bases. Key aspects of RNA specificity can be explained by the presence of intermolecular aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE structure represents one of the first steps towards understanding of the assembly of the cleavage and polyadenylation machinery at the atomic level.