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细菌RNA伴侣和类伴侣核糖调节因子:RNA介导的细胞代谢调控背后的机制

Bacterial RNA chaperones and chaperone-like riboregulators: behind the scenes of RNA-mediated regulation of cellular metabolism.

作者信息

Katsuya-Gaviria Kai, Paris Giulia, Dendooven Tom, Bandyra Katarzyna J

机构信息

Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.

Department of Structural Studies, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.

出版信息

RNA Biol. 2022;19(1):419-436. doi: 10.1080/15476286.2022.2048565. Epub 2021 Dec 31.

DOI:10.1080/15476286.2022.2048565
PMID:35438047
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9037510/
Abstract

In all domains of life, RNA chaperones safeguard and guide the fate of the cellular RNA pool. RNA chaperones comprise structurally diverse proteins that ensure proper folding, stability, and ribonuclease resistance of RNA, and they support regulatory activities mediated by RNA. RNA chaperones constitute a topologically diverse group of proteins that often present an unstructured region and bind RNA with limited nucleotide sequence preferences. In bacteria, three main proteins - Hfq, ProQ, and CsrA - have been shown to regulate numerous complex processes, including bacterial growth, stress response and virulence. Hfq and ProQ have well-studied activities as global chaperones with pleiotropic impact, while CsrA has a chaperone-like role with more defined riboregulatory function. Here, we describe relevant novel insights into their common features, including RNA binding properties, unstructured domains, and interplay with other proteins important to RNA metabolism.

摘要

在生命的所有领域中,RNA伴侣蛋白保护并引导细胞RNA库的命运。RNA伴侣蛋白由结构多样的蛋白质组成,这些蛋白质可确保RNA正确折叠、稳定并具有核糖核酸酶抗性,并且它们支持由RNA介导的调节活动。RNA伴侣蛋白构成了一组拓扑结构多样的蛋白质,它们通常具有一个无结构区域,并以有限的核苷酸序列偏好结合RNA。在细菌中,三种主要蛋白质——Hfq、ProQ和CsrA——已被证明可调节众多复杂过程,包括细菌生长、应激反应和毒力。Hfq和ProQ作为具有多效性影响的全局伴侣蛋白,其活性已得到充分研究,而CsrA具有类似伴侣蛋白的作用,其核糖调节功能更为明确。在这里,我们描述了对它们共同特征的相关新见解,包括RNA结合特性、无结构域以及与对RNA代谢重要的其他蛋白质的相互作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/2e6eaffe665b/KRNB_A_2048565_F0008_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/7d2475781b20/KRNB_A_2048565_F0001_OC.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/17c13144ef75/KRNB_A_2048565_F0005_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/f79eb97c7c07/KRNB_A_2048565_F0006_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/97941853ee33/KRNB_A_2048565_F0007_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/2e6eaffe665b/KRNB_A_2048565_F0008_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/7d2475781b20/KRNB_A_2048565_F0001_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/11947dd917e1/KRNB_A_2048565_F0002_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/be5e08236ac1/KRNB_A_2048565_F0003_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/fde85d956cca/KRNB_A_2048565_F0004_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/17c13144ef75/KRNB_A_2048565_F0005_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/f79eb97c7c07/KRNB_A_2048565_F0006_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/97941853ee33/KRNB_A_2048565_F0007_OC.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3804/9037510/2e6eaffe665b/KRNB_A_2048565_F0008_OC.jpg

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