The VrrA sRNA controls a stationary phase survival factor Vrp of Vibrio cholerae
2015 (English)In: RNA Biology, ISSN 1547-6286, E-ISSN 1555-8584, Vol. 12, no 2, 186-196 p.Article in journal (Refereed) Published
Small non-coding RNAs (sRNAs) are emerging regulatory elements in bacteria. The Vibrio cholerae sRNA VrrA has previously been shown to down-regulate outer membrane proteins (OmpA and OmpT) and biofilmmatrix protein (RbmC) by base-pairing with the 50 region of the corresponding mRNAs. In this study, we present an additional target of VrrA in V. cholerae, the mRNA coding for the ribosome binding protein Vrp. Vrp is homologous to ribosome-associated inhibitor A (RaiA) of Escherichia coli which facilitates stationary phase survival through ribosome hibernation. We show that VrrA downregulates Vrp protein synthesis by base-pairing to the 50 region of vrp mRNA and that the regulation requires the RNA chaperone protein, Hfq. We further demonstrate that Vrp is highly expressed during stationary phase growth and associates with the ribosome of V. cholerae. The effect of the Vrp protein in starvation survival is synergistic with that of the VC2530 protein, a homolog of the E. coli hibernation promoting factor HPF, suggesting a combined role for these proteins in ribosome hibernation in V. cholerae. Vrp and VC2530 are important for V. cholerae starvation survival under nutrient deficient conditions. While VC2530 is down-regulated in cells lacking vrrA, mutation of vrp results in VC2530 activation. This is the first report indicating a regulatory role for an sRNA, modulating stationary factors involved in bacterial ribosome hibernation.
Place, publisher, year, edition, pages
2015. Vol. 12, no 2, 186-196 p.
Hfq, Ribosome hibernation, sRNA, Vibrio cholerae, VrrA, Vrp
Cell and Molecular Biology
IdentifiersURN: urn:nbn:se:umu:diva-103572DOI: 10.1080/15476286.2015.1017211ISI: 000352238900009PubMedID: 25826569OAI: oai:DiVA.org:umu-103572DiVA: diva2:813762