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首页> 外文期刊>Journal of Molecular Biology >Recognition of enolase in the Escherichia coli RNA degradosome
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Recognition of enolase in the Escherichia coli RNA degradosome

机译：大肠杆菌RNA降解体中烯醇化酶的识别

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摘要

In Escherichia coli, the glycolytic enzyme enolase is a component of the RNA degradosome, which is an RNase E mediated assembly involved in RNA processing and transcript turnover. The recruitment of enolase by the RNA degradosome has been implicated in the turnover of certain transcripts, and it is mediated by a small segment of roughly a dozen residues that lie within a natively unstructured sub-domain of RNase E. Here, we present the crystal structure of enolase in complex with its recognition site from RNase E at 1.6 angstrom resolution. A single molecule of the RNase E peptide binds asymmetrically in a conserved cleft at the interface of the enolase dimer. The recognition site is well conserved in RNase E homologues in a subfamily of the gamma-proteobacteria, including enzymes from pathogens such as Yersinia Pestis, Vibrio cholera and Salmonella sp. We suggest that enolase is recruited into putative RNA degradosome machinery in these bacilli, where it plays common regulatory functions. (c) 2006 Elsevier Ltd. All rights reserved.
机译：在大肠杆菌中，糖酵解烯醇酶是RNA降解体的组成部分，RNA降解体是一种RNA酶E介导的装配，涉及RNA加工和转录物更新。 RNA降解体对烯醇酶的募集与某些转录物的转换有关，它由一小部分大约一打的残基介导，这些残基位于RNase E的天然非结构化子域内。在这里，我们介绍晶体烯醇酶的结构，其识别位点来自RNase E，分辨率为1.6埃。 RNase E肽的单个分子在烯醇酶二聚体界面的保守裂隙中不对称结合。识别位点在γ-变形细菌亚科的RNase E同源物中是非常保守的，包括来自病原体（如耶尔森菌，霍乱弧菌和沙门氏菌）的酶。我们建议将烯醇酶募集到这些杆菌中假定的RNA降解体机制中，在其中发挥共同的调节功能。 （c）2006 Elsevier Ltd.保留所有权利。

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