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dc.contributor.authorGonzalez, Gen
dc.contributor.authorHardwick, Stevenen
dc.contributor.authorMaslen, SLen
dc.contributor.authorSkehel, JMen
dc.contributor.authorHolmqvist, Een
dc.contributor.authorVogel, Jen
dc.contributor.authorBateman, Aen
dc.contributor.authorLuisi, Benen
dc.contributor.authorBroadhurst, Billen
dc.date.accessioned2017-04-28T09:36:32Z
dc.date.available2017-04-28T09:36:32Z
dc.date.issued2017-05-01en
dc.identifier.issn1355-8382
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/263862
dc.description.abstractThe protein ProQ has recently been identified as a global RNA chaperone in $\textit{Salmonella}$, and a similar role is anticipated for its numerous homologues in divergent bacterial species. We report the solution structure of $\textit{Escherichia coli}$ ProQ, revealing an N-terminal FinO-like domain, a C-terminal domain that unexpectedly has a Tudor-domain fold commonly found in eukaryotes, and an elongated bridging intra-domain linker that is flexible but nonetheless incompressible. Structure based sequence analysis suggests that the Tudor domain was acquired through horizontal gene transfer and gene fusion to the ancestral FinO-like domain. Through a combination of biochemical and biophysical approaches, we have mapped putative RNA binding surfaces on all three domains of ProQ and modelled the protein's conformation in the apo and RNA-bound forms. Taken together, these data suggest how the FinO, Tudor and linker domains of ProQ cooperate to recognise complex RNA structures and serve to promote RNA-mediated regulation.
dc.description.sponsorshipG.M.G. was supported by a Gates Cambridge Scholarship. B.F.L., G.M.G., and S.W.H. are supported by the Wellcome Trust.
dc.languageengen
dc.language.isoenen
dc.publisherCold Spring Harbor
dc.rightsAttribution 4.0 Internationalen
dc.rightsAttribution 4.0 Internationalen
dc.rightsAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectFinOen
dc.subjectRNA chaperoneen
dc.subjectprotein-RNA interactionsen
dc.subjectregulatory RNAen
dc.subjectriboregulationen
dc.titleStructure of the $\textit{Escherichia coli}$ ProQ RNA chaperone proteinen
dc.typeArticle
prism.endingPage711
prism.publicationDate2017en
prism.publicationNameRNAen
prism.startingPage696
prism.volume23en
dc.identifier.doi10.17863/CAM.9242
dcterms.dateAccepted2017-02-03en
rioxxterms.versionofrecord10.1261/rna.060343.116en
rioxxterms.versionVoRen
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2017-05-01en
dc.contributor.orcidHardwick, Steven [0000-0001-9246-1864]
dc.contributor.orcidLuisi, Ben [0000-0003-1144-9877]
dc.contributor.orcidBroadhurst, Bill [0000-0002-0264-4593]
dc.identifier.eissn1469-9001
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idWellcome Trust (094229/Z/10/Z)
pubs.funder-project-idWELLCOME TRUST (200873/Z/16/Z)
cam.issuedOnline2017-02-13en
cam.orpheus.successThu Jan 30 12:53:57 GMT 2020 - The item has an open VoR version.*
rioxxterms.freetoread.startdate2100-01-01


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