Interrogation of RNA-protein interaction dynamics in bacterial growth

Interrogation of RNA-protein interaction dynamics in bacterial growth
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细菌生长中 RNA-蛋白质相互作用动力学的探究

DOI:
10.1101/2023.07.03.547468
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发表时间:
2023
期刊:
--
影响因子:
--
通讯作者:
Monti M
Monti M
中科院分区:
--
文献类型:
--
作者:
Monti M

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表征RNA-蛋白质相互作用动力学是了解细菌如何响应其环境的基础。在这项研究中,我们分析了91%的大肠杆菌表达的蛋白质组的动态和271 RNA结合蛋白(RBP)在不同生长阶段的RNA相互作用特性。我们发现,68%的RBP在不同的生长阶段与RNA有差异地结合,并且与细菌的RBP(包括一种ncRNA结合蛋白YfiF)一样,有17种以前未注释的蛋白质。虽然这些新的RBP主要存在于变形菌中,但其中两种是与罕见代谢紊乱相关的人类线粒体蛋白的直系同源物。此外,我们揭示了新的RBP功能的蛋白质,如分子伴侣HtpG,一种新的固定相tRNA结合蛋白。首次对细菌RBPome的动力学进行了研究,展示了这种方法如何揭示未表征蛋白质的功能,并确定细胞生长的关键RNA-蛋白质相互作用,这可能会为新的抗菌疗法提供信息。
Characterising RNA–protein interaction dynamics is fundamental to understand how bacteria respond to their environment. In this study, we have analysed the dynamics of 91% of theEscherichia coliexpressed proteome and the RNA-interaction properties of 271 RNA-binding proteins (RBPs) at different growth phases. We find that 68% of RBPs differentially bind RNA across growth phases and characterise 17 previously unannotated proteins as bacterial RBPs including YfiF, a ncRNA-binding protein. While these new RBPs are mostly present in Proteobacteria, two of them are orthologs of human mitochondrial proteins associated with rare metabolic disorders. Moreover, we reveal novel RBP functions for proteins such as the chaperone HtpG, a new stationary phase tRNA-binding protein. For the first time, the dynamics of the bacterial RBPome have been interrogated, showcasing how this approach can reveal the function of uncharacterised proteins and identify critical RNA–protein interactions for cell growth which could inform new antimicrobial therapies.
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