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dc.contributor.authorSmirnov, Alexandre
dc.contributor.authorWang, Chuan
dc.contributor.authorDrewry, Lisa L
dc.contributor.authorVogel, Jörg
dc.date.accessioned2018-09-24T09:11:07Z
dc.date.available2018-09-24T09:11:07Z
dc.date.issued2017-04-13
dc.identifier.issn1460-2075
dc.identifier.pmid28336682
dc.identifier.doi10.15252/embj.201696127
dc.identifier.urihttp://hdl.handle.net/10033/621490
dc.description.abstractResearch into post-transcriptional control of mRNAs by small noncoding RNAs (sRNAs) in the model bacteria Escherichia coli and Salmonella enterica has mainly focused on sRNAs that associate with the RNA chaperone Hfq. However, the recent discovery of the protein ProQ as a common binding partner that stabilizes a distinct large class of structured sRNAs suggests that additional RNA regulons exist in these organisms. The cellular functions and molecular mechanisms of these new ProQ-dependent sRNAs are largely unknown. Here, we report in Salmonella Typhimurium the mode-of-action of RaiZ, a ProQ-dependent sRNA that is made from the 30 end of the mRNA encoding ribosome-inactivating protein RaiA. We show that RaiZ is a base-pairing sRNA that represses in trans the mRNA of histone-like protein HU-a. RaiZ forms an RNA duplex with the ribosome-binding site of hupA mRNA, facilitated by ProQ, to prevent 30S ribosome loading and protein synthesis of HU-a. Similarities and differences between ProQ- and Hfqmediated regulation will be discussed.en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subjectHU‐αen_US
dc.subjectProQen_US
dc.subjectRaiZen_US
dc.subjectsmall RNAen_US
dc.subjecttranslation inhibitionen_US
dc.titleMolecular mechanism of mRNA repression in by a ProQ-dependent small RNA.en_US
dc.typeArticleen_US
dc.contributor.departmentHIRI, Helmoltz-Institut für RNA-basierteInfektionsforschung, Josef-Schneider-Strasse 2, 97080 Würzburg, Germany.en_US
refterms.dateFOA2018-09-24T09:11:07Z
dc.source.journaltitleThe EMBO journal


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