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dc.contributor.authorGerovac, Milan
dc.contributor.authorEl Mouali, Youssef
dc.contributor.authorKuper, Jochen
dc.contributor.authorKisker, Caroline
dc.contributor.authorBarquist, Lars
dc.contributor.authorVogel, Jörg
dc.date.accessioned2020-10-26T10:55:18Z
dc.date.available2020-10-26T10:55:18Z
dc.date.issued2020-07-09
dc.identifier.citationRNA. 2020 Oct;26(10):1448-1463. doi: 10.1261/rna.076992.120.en_US
dc.identifier.pmid32646969
dc.identifier.doi10.1261/rna.076992.120
dc.identifier.urihttp://hdl.handle.net/10033/622535
dc.description.abstractRNA-binding proteins (RBPs) play important roles in bacterial gene expression and physiology but their true number and functional scope remain little understood even in model microbes. To advance global RBP discovery in bacteria, we here establish glycerol gradient sedimentation with RNase treatment and mass spectrometry (GradR). Applied to Salmonella enterica, GradR confirms many known RBPs such as CsrA, Hfq, and ProQ by their RNase-sensitive sedimentation profiles, and discovers the FopA protein as a new member of the emerging family of FinO/ProQ-like RBPs. FopA, encoded on resistance plasmid pCol1B9, primarily targets a small RNA associated with plasmid replication. The target suite of FopA dramatically differs from the related global RBP ProQ, revealing context-dependent selective RNA recognition by FinO-domain RBPs. Numerous other unexpected RNase-induced changes in gradient profiles suggest that cellular RNA helps to organize macromolecular complexes in bacteria. By enabling poly(A)-independent generic RBP discovery, GradR provides an important element in the quest to build a comprehensive catalog of microbial RBPs.en_US
dc.language.isoenen_US
dc.publisherCold Spring Habor Laboratory Press and RNA Societyen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectCsrAen_US
dc.subjectFinO/ProQ proteinen_US
dc.subjectFopAen_US
dc.subjectHfqen_US
dc.subjectRNA-binding proteinen_US
dc.subjectRNaseen_US
dc.titleGlobal discovery of bacterial RNA-binding proteins by RNase-sensitive gradient profiles reports a new FinO domain protein.en_US
dc.typeArticleen_US
dc.identifier.eissn1469-9001
dc.contributor.departmentHIRI, Helmholtz-Institut für RNA-basierte Infektionsforschung, Josef-Shneider Strasse 2, 97080 Würzburg, Germany.en_US
dc.identifier.journalRNA (New York, N.Y.)en_US
dc.source.volume26
dc.source.issue10
dc.source.beginpage1448
dc.source.endpage1463
refterms.dateFOA2020-10-26T10:55:18Z
dc.source.journaltitleRNA (New York, N.Y.)
dc.source.countryUnited States


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