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dc.contributor.authorBravo, Jack P K
dc.contributor.authorBartnik, Kira
dc.contributor.authorVenditti, Luca
dc.contributor.authorAcker, Julia
dc.contributor.authorGail, Emma H
dc.contributor.authorColyer, Alice
dc.contributor.authorDavidovich, Chen
dc.contributor.authorLamb, Don C
dc.contributor.authorTuma, Roman
dc.contributor.authorCalabrese, Antonio N
dc.contributor.authorBorodavka, Alexander
dc.date.accessioned2021-11-08T01:51:47Z
dc.date.available2021-11-08T01:51:47Z
dc.date.issued2021-10-01
dc.identifier.issn0027-8424
dc.identifier.otherPMC8521686
dc.identifier.other34615715
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/330417
dc.description.abstractRotavirus genomes are distributed between 11 distinct RNA molecules, all of which must be selectively copackaged during virus assembly. This likely occurs through sequence-specific RNA interactions facilitated by the RNA chaperone NSP2. Here, we report that NSP2 autoregulates its chaperone activity through its C-terminal region (CTR) that promotes RNA-RNA interactions by limiting its helix-unwinding activity. Unexpectedly, structural proteomics data revealed that the CTR does not directly interact with RNA, while accelerating RNA release from NSP2. Cryo-electron microscopy reconstructions of an NSP2-RNA complex reveal a highly conserved acidic patch on the CTR, which is poised toward the bound RNA. Virus replication was abrogated by charge-disrupting mutations within the acidic patch but completely restored by charge-preserving mutations. Mechanistic similarities between NSP2 and the unrelated bacterial RNA chaperone Hfq suggest that accelerating RNA dissociation while promoting intermolecular RNA interactions may be a widespread strategy of RNA chaperone recycling.
dc.languageeng
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceessn: 1091-6490
dc.sourcenlmid: 7505876
dc.subjectRotavirus
dc.subjectRibonucleoproteins
dc.subjectGenome Assembly
dc.subjectRna Chaperones
dc.titleStructural basis of rotavirus RNA chaperone displacement and RNA annealing.
dc.typeArticle
dc.date.updated2021-11-08T01:51:46Z
prism.issueIdentifier41
prism.publicationNameProceedings of the National Academy of Sciences of the United States of America
prism.volume118
dc.identifier.doi10.17863/CAM.77860
rioxxterms.versionofrecord10.1073/pnas.2100198118
rioxxterms.versionVoR
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidBartnik, Kira [0000-0002-6951-7206]
dc.contributor.orcidAcker, Julia [0000-0002-6422-6514]
dc.contributor.orcidColyer, Alice [0000-0002-1880-1995]
dc.contributor.orcidDavidovich, Chen [0000-0002-1085-6094]
dc.contributor.orcidLamb, Don C [0000-0002-0232-1903]
dc.contributor.orcidCalabrese, Antonio N [0000-0003-2437-7761]
dc.contributor.orcidBorodavka, Alexander [0000-0002-5729-2687]
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/M011151/1, BB/M012573/1)
pubs.funder-project-idWellcome Trust (094232, 208385/Z/17/Z, 213437/Z/18/Z, 108466/Z/15/Z, 220628/Z/20/Z)


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