The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E.

The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E.
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DOI:
10.1093/nar/gkac1228
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发表时间:
2023-01-11
影响因子:
14.9
通讯作者:
McDowall, Kenneth J.
McDowall, Kenneth J.
中科院分区:
生物学2区
文献类型:
--
作者:
Clarke, Justin E.;Sabharwal, Kiran;Kime, Louise;McDowall, Kenneth J.

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RNase E是一种核糖核酸内切酶,存在于许多细菌中,包括重要的人类病原体。在大肠杆菌中,它已被证明在参与翻译的所有类型的RNA的成熟和mRNA降解的起始中起主要作用。因此,RNase E裂解的主要决定因素的知识是我们理解和操纵细菌基因表达的核心。我们在这里表明,RNase E与结构化RNA元件的结合对于tRNA的加工至关重要,可以激活催化作用,并且在mRNA降解中可能很重要。RNase E对结构元件的识别是由最近发现的远离与催化相关的结构域的凹槽介导的。这条沟的功能在这里显示是必不可少的E。大肠杆菌细胞的活力,并可能代表了一个关键点的进化分歧从旁系同源的RNase G家族,我们表明缺乏氨基酸残基保守的RNA结合沟的成员的RNase E家族。总的来说,这项工作提供了新的见解,RNA酶E的识别和切割的RNA,并提供了进一步了解的基础上,RNA酶E的必要性,在E。杆菌
RNase E is an endoribonuclease found in many bacteria, including important human pathogens. Within Escherichia coli, it has been shown to have a major role in both the maturation of all classes of RNA involved in translation and the initiation of mRNA degradation. Thus, knowledge of the major determinants of RNase E cleavage is central to our understanding and manipulation of bacterial gene expression. We show here that the binding of RNase E to structured RNA elements is crucial for the processing of tRNA, can activate catalysis and may be important in mRNA degradation. The recognition of structured elements by RNase E is mediated by a recently discovered groove that is distant from the domains associated with catalysis. The functioning of this groove is shown here to be essential for E. coli cell viability and may represent a key point of evolutionary divergence from the paralogous RNase G family, which we show lack amino acid residues conserved within the RNA-binding groove of members of the RNase E family. Overall, this work provides new insights into the recognition and cleavage of RNA by RNase E and provides further understanding of the basis of RNase E essentiality in E. coli.
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