Evidence map›Paper›PMID 34615715›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Structural basis of rotavirus RNA chaperone displacement and RNA annealing.

Jack P K Bravo, Kira Bartnik, Luca Venditti, Julia Acker, Emma H Gail, Alice Colyer, Chen Davidovich, Don C Lamb, Roman Tuma, Antonio N Calabrese and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Phosphorylation enables allosteric control of a viral condensate.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 4 countries.

Jack P K BravoDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom.
Kira BartnikDepartment of Chemistry, Center for NanoScience, Nanosystems Initiative Munich, Centre for Integrated Protein Science Munich, Ludwig Maximilian University of Munich, D-81377 Munich, Germany.ORCID 0000-0002-6951-7206
Luca VendittiDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom.
Julia AckerDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom.ORCID 0000-0002-6422-6514
Emma H GailDepartment of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.
Alice ColyerAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT Leeds, United Kingdom.ORCID 0000-0002-1880-1995
Chen DavidovichDepartment of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, VIC 3800, Australia.ORCID 0000-0002-1085-6094
Don C LambDepartment of Chemistry, Center for NanoScience, Nanosystems Initiative Munich, Centre for Integrated Protein Science Munich, Ludwig Maximilian University of Munich, D-81377 Munich, Germany.ORCID 0000-0002-0232-1903
Roman TumaAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT Leeds, United Kingdom.
Antonio N CalabreseAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT Leeds, United Kingdom.ORCID 0000-0003-2437-7761
Alexander BorodavkaDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom; ab2677@cam.ac.uk.ORCID 0000-0002-5729-2687
University of Leeds · GBAustralian Research Council · AUCenter for Integrated Protein Science Munich · DEUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011151/1Biotechnology and Biological Sciences Research Council BB/M012573/1Wellcome Trust 108466/Z/15/ZWellcome Trust 208385/Z/17/ZWellcome Trust 213437/Z/18/ZWellcome Trust 220628Wellcome Trust 220628/Z/20/Z
6 · The paper itself

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.

Indexed as

Cryoelectron MicroscopyGenome, ViralModels, MolecularMolecular ChaperonesRibonucleoproteinsRNA-Binding ProteinsRNA FoldingRNA, ViralRotavirusViral Genome PackagingViral Nonstructural ProteinsMolecular ChaperonesRibonucleoproteinsRNA-Binding ProteinsRNA, ViralViral Nonstructural Proteinsgenome assemblyribonucleoproteinsRNA chaperonesrotavirus

Identifiers

PMID34615715
PMCPMC8521686
OpenAlexW3201894557

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.