Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Jul 12:11:604511.
doi: 10.3389/fcimb.2021.604511. eCollection 2021.

Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity

Affiliations
Review

Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity

Louise Djapgne et al. Front Cell Infect Microbiol. .

Abstract

Bacterial small RNAs (sRNAs) are critical post-transcriptional regulators that exert broad effects on cell physiology. One class of sRNAs, referred to as trans-acting sRNAs, base-pairs with mRNAs to cause changes in their stability or translation. Another class of sRNAs sequesters RNA-binding proteins that in turn modulate mRNA expression. RNA chaperones play key roles in these regulatory events by promoting base-pairing of sRNAs to mRNAs, increasing the stability of sRNAs, inducing conformational changes on mRNA targets upon binding, or by titrating sRNAs away from their primary targets. In pathogenic bacteria, sRNAs and their chaperones exert broad impacts on both cell physiology and virulence, highlighting the central role of these systems in pathogenesis. This review provides an overview of the growing number and roles of these chaperone proteins in sRNA regulation, highlighting how these proteins contribute to bacterial pathogenesis.

Keywords: Crc; FinO; Hfq; ProQ; RsmA; sRNA.

PubMed Disclaimer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Gene regulation by sRNA and Hfq in bacteria. Hfq can protect sRNAs from ribonuclease cleavage (A) or recruit RNases to degrade of sRNA-mRNA complexes (B). Hfq can also promote sRNA binding that precludes access of the ribosome to the Shine Dalgarno (SD) to inhibit translation (C), or promote sRNA binding that releases inhibitory structures to increase translation (D).
Figure 2
Figure 2
Crystal structure of the P. aeruginosa Hfq protein adapted from 1U1S.PDB: its proximal face, its distal face, and its rim/lateral face indicated. Also indicated in yellow (R16), orange (K16), and magenta (R19) are the acidic amino acid residues on the rim (Nikulin et al., 2005).

References

    1. Aiba H. (2007). Mechanism of RNA Silencing by Hfq-Binding Small RNAs. Curr. Opin. Microbiol. 10, 134–139. 10.1016/j.mib.2007.03.010 - DOI - PubMed
    1. Argaman L., Elgrably-Weiss M., Hershko T., Vogel J., Altuvia S. (2012). Rela Protein Stimulates the Activity of RyhB Small RNA by Acting on RNA-Binding Protein Hfq. Proc. Natl. Acad. Sci. U. S. A. 109, 4621–4626. 10.1073/pnas.1113113109 - DOI - PMC - PubMed
    1. Arluison V., Hohng S., Roy R., Pellegrini O., Regnier P., Ha T. (2007). Spectroscopic Observation of RNA Chaperone Activities of Hfq in Post-Transcriptional Regulation by a Small Non-Coding RNA. Nucleic Acids Res. 35, 999–1006. 10.1093/nar/gkl1124 - DOI - PMC - PubMed
    1. Arthur D. C., Edwards R. A., Tsutakawa S., Tainer J. A., Frost L. S., Glover J. N. (2011). Mapping Interactions Between the RNA Chaperone FinO and Its RNA Targets. Nucleic Acids Res. 39, 4450–4463. 10.1093/nar/gkr025 - DOI - PMC - PubMed
    1. Attaiech L., Boughammoura A., Brochier-Armanet C., Allatif O., Peillard-Fiorente F., Edwards R. A., et al. . (2016). Silencing of Natural Transformation by an RNA Chaperone and a Multitarget Small RNA. Proc. Natl. Acad. Sci. U. S. A. 113, 8813–8818. 10.1073/pnas.1601626113 - DOI - PMC - PubMed

Publication types

MeSH terms

LinkOut - more resources