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Article

Binding of the RNA Chaperone Hfq on Target mRNAs Promotes the Small RNA RyhB-Induced Degradation in Escherichia coli

1
CRCHUS, RNA Group, Department of Biochemistry and Functional Genomics, Faculty of Medicine and Health Sciences, Université de Sherbrooke, 3201 Jean Mignault Street, Sherbrooke, QC J1E 4K8, Canada
2
RNA architecture and reactivity Unit, Université de Strasbourg, CNRS, ARN UPR 9002, F-67000 Strasbourg, France
3
Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, 929 E. 57 St., Chicago, IL 60637, USA
4
Department of Microbiology, University of Illinois at Urbana-Champaign, 601 S Goodwin Ave., Urbana, IL 61801, USA
*
Authors to whom correspondence should be addressed.
Co-first authors.
Main correspondence.
Academic Editor: George A. Calin
Non-Coding RNA 2021, 7(4), 64; https://doi.org/10.3390/ncrna7040064
Received: 28 June 2021 / Revised: 3 September 2021 / Accepted: 20 September 2021 / Published: 28 September 2021
(This article belongs to the Special Issue Non-coding RNA: 5th Anniversary)
Many RNA-RNA interactions depend on molecular chaperones to form and remain stable in living cells. A prime example is the RNA chaperone Hfq, which is a critical effector involved in regulatory interactions between small RNAs (sRNAs) and cognate target mRNAs in Enterobacteriaceae. While there is a great deal of in vitro biochemical evidence supporting the model that Hfq enhances rates or affinities of sRNA:mRNA interactions, there is little corroborating in vivo evidence. Here we used in vivo tools including reporter genes, co-purification assays, and super-resolution microscopy to analyze the role of Hfq in RyhB-mediated regulation, and we found that Hfq is often unnecessary for efficient RyhB:mRNA complex formation in vivo. Remarkably, our data suggest that a primary function of Hfq is to promote RyhB-induced cleavage of mRNA targets by RNase E. Moreover, our work indicates that Hfq plays a more limited role in dictating regulatory outcomes following sRNAs RybB and DsrA complex formation with specific target mRNAs. Our investigation helps evaluate the roles played by Hfq in some RNA-mediated regulation. View Full-Text
Keywords: small RNA (sRNA); Hfq; RNase E; sRNA-induced degradation; super-resolution imaging; RNA chaperone; Hfq binding site small RNA (sRNA); Hfq; RNase E; sRNA-induced degradation; super-resolution imaging; RNA chaperone; Hfq binding site
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MDPI and ACS Style

Lalaouna, D.; Prévost, K.; Park, S.; Chénard, T.; Bouchard, M.-P.; Caron, M.-P.; Vanderpool, C.K.; Fei, J.; Massé, E. Binding of the RNA Chaperone Hfq on Target mRNAs Promotes the Small RNA RyhB-Induced Degradation in Escherichia coli. Non-Coding RNA 2021, 7, 64. https://doi.org/10.3390/ncrna7040064

AMA Style

Lalaouna D, Prévost K, Park S, Chénard T, Bouchard M-P, Caron M-P, Vanderpool CK, Fei J, Massé E. Binding of the RNA Chaperone Hfq on Target mRNAs Promotes the Small RNA RyhB-Induced Degradation in Escherichia coli. Non-Coding RNA. 2021; 7(4):64. https://doi.org/10.3390/ncrna7040064

Chicago/Turabian Style

Lalaouna, David, Karine Prévost, Seongjin Park, Thierry Chénard, Marie-Pier Bouchard, Marie-Pier Caron, Carin K. Vanderpool, Jingyi Fei, and Eric Massé. 2021. "Binding of the RNA Chaperone Hfq on Target mRNAs Promotes the Small RNA RyhB-Induced Degradation in Escherichia coli" Non-Coding RNA 7, no. 4: 64. https://doi.org/10.3390/ncrna7040064

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