Structural basis of rotavirus RNA chaperone displacement and RNA annealing.
dc.contributor.author | Bravo, Jack P K | |
dc.contributor.author | Bartnik, Kira | |
dc.contributor.author | Venditti, Luca | |
dc.contributor.author | Acker, Julia | |
dc.contributor.author | Gail, Emma H | |
dc.contributor.author | Colyer, Alice | |
dc.contributor.author | Davidovich, Chen | |
dc.contributor.author | Lamb, Don C | |
dc.contributor.author | Tuma, Roman | |
dc.contributor.author | Calabrese, Antonio N | |
dc.contributor.author | Borodavka, Alexander | |
dc.date.accessioned | 2021-11-08T01:51:47Z | |
dc.date.available | 2021-11-08T01:51:47Z | |
dc.date.issued | 2021-10-01 | |
dc.identifier.issn | 0027-8424 | |
dc.identifier.other | PMC8521686 | |
dc.identifier.other | 34615715 | |
dc.identifier.uri | https://www.repository.cam.ac.uk/handle/1810/330417 | |
dc.description.abstract | Rotavirus 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.language | eng | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.source | essn: 1091-6490 | |
dc.source | nlmid: 7505876 | |
dc.subject | Rotavirus | |
dc.subject | Ribonucleoproteins | |
dc.subject | Genome Assembly | |
dc.subject | Rna Chaperones | |
dc.title | Structural basis of rotavirus RNA chaperone displacement and RNA annealing. | |
dc.type | Article | |
dc.date.updated | 2021-11-08T01:51:46Z | |
prism.issueIdentifier | 41 | |
prism.publicationName | Proceedings of the National Academy of Sciences of the United States of America | |
prism.volume | 118 | |
dc.identifier.doi | 10.17863/CAM.77860 | |
rioxxterms.versionofrecord | 10.1073/pnas.2100198118 | |
rioxxterms.version | VoR | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.contributor.orcid | Bartnik, Kira [0000-0002-6951-7206] | |
dc.contributor.orcid | Acker, Julia [0000-0002-6422-6514] | |
dc.contributor.orcid | Colyer, Alice [0000-0002-1880-1995] | |
dc.contributor.orcid | Davidovich, Chen [0000-0002-1085-6094] | |
dc.contributor.orcid | Lamb, Don C [0000-0002-0232-1903] | |
dc.contributor.orcid | Calabrese, Antonio N [0000-0003-2437-7761] | |
dc.contributor.orcid | Borodavka, Alexander [0000-0002-5729-2687] | |
pubs.funder-project-id | Biotechnology and Biological Sciences Research Council (BB/M011151/1, BB/M012573/1) | |
pubs.funder-project-id | Wellcome Trust (094232, 208385/Z/17/Z, 213437/Z/18/Z, 108466/Z/15/Z, 220628/Z/20/Z) |
Files in this item
This item appears in the following Collection(s)
-
Jisc Publications Router
This collection holds Cambridge publications received from the Jisc Publications Router