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dc.contributor.authorBauriedl, Saskia
dc.contributor.authorGerovac, Milan
dc.contributor.authorHeidrich, Nadja
dc.contributor.authorBischler, Thorsten
dc.contributor.authorBarquist, Lars
dc.contributor.authorVogel, Jörg
dc.contributor.authorSchoen, Christoph
dc.date.accessioned2021-04-27T13:57:22Z
dc.date.available2021-04-27T13:57:22Z
dc.date.issued2020-06-04
dc.identifier.citationNat Commun. 2020 Jun 4;11(1):2823. doi: 10.1038/s41467-020-16650-6.en_US
dc.identifier.pmid32499480
dc.identifier.doi10.1038/s41467-020-16650-6
dc.identifier.urihttp://hdl.handle.net/10033/622847
dc.description.abstractFinO-domain proteins are a widespread family of bacterial RNA-binding proteins with regulatory functions. Their target spectrum ranges from a single RNA pair, in the case of plasmid-encoded FinO, to global RNA regulons, as with enterobacterial ProQ. To assess whether the FinO domain itself is intrinsically selective or promiscuous, we determine in vivo targets of Neisseria meningitidis, which consists of solely a FinO domain. UV-CLIP-seq identifies associations with 16 small non-coding sRNAs and 166 mRNAs. Meningococcal ProQ predominantly binds to highly structured regions and generally acts to stabilize its RNA targets. Loss of ProQ alters transcript levels of >250 genes, demonstrating that this minimal ProQ protein impacts gene expression globally. Phenotypic analyses indicate that ProQ promotes oxidative stress resistance and DNA damage repair. We conclude that FinO domain proteins recognize some abundant type of RNA shape and evolve RNA binding selectivity through acquisition of additional regions that constrain target recognition.en_US
dc.language.isoenen_US
dc.publisherNature Researchen_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.titleThe minimal meningococcal ProQ protein has an intrinsic capacity for structure-based global RNA recognition.en_US
dc.typeArticleen_US
dc.identifier.eissn2041-1723
dc.contributor.departmentHIRI, Helmholtz-Institut für RNA-basierte Infektionsforschung, Josef-Shneider Strasse 2, 97080 Würzburg, Germany.en_US
dc.identifier.journalNature communicationsen_US
dc.source.volume11
dc.source.issue1
dc.source.beginpage2823
dc.source.endpage
refterms.dateFOA2021-04-27T13:57:22Z
dc.source.journaltitleNature communications
dc.source.countryEngland


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Attribution 4.0 International
Except where otherwise noted, this item's license is described as Attribution 4.0 International