Evidence map›Paper›PMID 23318955›Full record

ArticleJournal of molecular biology2013

Sequence-specific, RNA-protein interactions overcome electrostatic barriers preventing assembly of satellite tobacco necrosis virus coat protein.

Robert J Ford, Amy M Barker, Saskia E Bakker, Robert H Coutts, Neil A Ranson, Simon E V Phillips, Arwen R Pearson, Peter G Stockley

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Virus Isoelectric Point Estimation: Theories and Methods.Applied and environmental microbiology · 2021
    Review
  12. Article
  13. Genome organization and interaction with capsid protein in a multipartite RNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Varieties of charge distributions in coat proteins of ssRNA+  viruses.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  19. Rewriting nature's assembly manual for a ssRNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

8 authors at 3 institutions in 1 country.

Robert J FordAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Amy M Barker
Saskia E Bakker
Robert H Coutts
Neil A Ranson
Simon E V Phillips
Arwen R Pearson
Peter G Stockley
University of Leeds · GBImperial College London · GBResearch Complex at Harwell · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 062164Wellcome Trust 083105/Z/07/ZWellcome Trust 090932/Z/09/Z
6 · The paper itself

Abstract

We have examined the roles of RNA-coat protein (CP) interactions in the assembly of satellite tobacco necrosis virus (STNV). The viral genomic RNA encodes only the CP, which comprises a β-barrel domain connected to a positively charged N-terminal extension. In the previous crystal structures of this system, the first 11 residues of the protein are disordered. Using variants of an RNA aptamer sequence isolated against the CP, B3, we have studied the sequence specificity of RNA-induced assembly. B3 consists of a stem-loop presenting the tetra-loop sequence ACAA. There is a clear preference for RNAs encompassing this loop sequence, as measured by the yield of T=1 capsids, which is indifferent to sequences within the stem. The B3-containing virus-like particle has been crystallised and its structure was determined to 2.3Å. A lower-resolution map encompassing density for the RNA has also been calculated. The presence of B3 results in increased ordering of the N-terminal helices located at the particle 3-fold axes, which extend by roughly one and a half turns to encompass residues 8-11, including R8 and K9. Under assembly conditions, STNV CP in the absence of RNA is monomeric and does not self-assemble. These facts suggest that a plausible model for assembly initiation is the specific RNA-induced stabilisation of a trimeric capsomere. The basic nature of the helical extension suggests that electrostatic repulsion between CPs prevents assembly in the absence of RNA and that this barrier is overcome by correct placement of appropriately orientated helical RNA stems. Such a mechanism would be consistent with the data shown here for assembly with longer RNA fragments, including an STNV genome. The results are discussed in light of a first stage of assembly involving compaction of the genomic RNA driven by multiple RNA packaging signal-CP interactions.

Indexed as

Amino Acid SequenceBinding SitesCapsidCapsid ProteinsGenome, ViralModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein ConformationRNA, ViralTobacco necrosis satellite virusCapsid Proteinscoat protein, Tobacco necrosis virus (Nebraska)RNA, Viral

Identifiers

PMID23318955
PMCPMC3593212
OpenAlexW2075663882

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.