Evidence map›Paper›PMID 26984530›Full record

ArticleNucleic acids research2016

An RNA trapping mechanism in Alphavirus mRNA promotes ribosome stalling and translation initiation.

René Toribio, Irene Díaz-López, Jasminka Boskovic, Iván Ventoso

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. 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
2.3field-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

30 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  7. Review
  8. Review
  9. Tailor made: the art of therapeutic mRNA design.Nature reviews. Drug discovery · 2024
    Review
  10. Review
  11. Article
  12. Ribosomal control in RNA virus-infected cells.Frontiers in microbiology · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Translational control of coronaviruses.Nucleic acids research · 2020
    Review
  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

4 authors at 3 institutions in 1 country.

René ToribioCentro de Biología Molecular 'Severo Ochoa' (CSIC-UAM) and Departamento de Biología Molecular, Universidad Autónoma de Madrid (UAM), Madrid, Spain.
Irene Díaz-LópezCentro de Biología Molecular 'Severo Ochoa' (CSIC-UAM) and Departamento de Biología Molecular, Universidad Autónoma de Madrid (UAM), Madrid, Spain.
Jasminka BoskovicStructural Biology and Biocomputing Programme, Electron Microscopy Unit, Spanish Nacional Cancer Research Center (CNIO), 28029 Madrid, Spain.
Iván VentosoCentro de Biología Molecular 'Severo Ochoa' (CSIC-UAM) and Departamento de Biología Molecular, Universidad Autónoma de Madrid (UAM), Madrid, Spain iventoso@cbm.csic.es.
Universidad Autónoma de Madrid · ESCentro de Biología Molecular Severo Ochoa · ESCentro de Investigación del Cáncer · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During translation initiation, eukaryotic initiation factor 2 (eIF2) delivers the Met-tRNA to the 40S ribosomal subunit to locate the initiation codon (AUGi) of mRNA during the scanning process. Stress-induced eIF2 phosphorylation leads to a general blockade of translation initiation and represents a key antiviral pathway in mammals. However, some viral mRNAs can initiate translation in the presence of phosphorylated eIF2 via stable RNA stem-loop structures (DLP; Downstream LooP) located in their coding sequence (CDS), which promote 43S preinitiation complex stalling on the initiation codon. We show here that during the scanning process, DLPs of Alphavirus mRNA become trapped in ES6S region (680-914 nt) of 18S rRNA that are projected from the solvent side of 40S subunit. This trapping can lock the progress of the 40S subunit on the mRNA in a way that places the upstream initiator AUGi on the P site of 40S subunit, obviating the participation of eIF2. Notably, the DLP structure is released from 18S rRNA upon 60S ribosomal subunit joining, suggesting conformational changes in ES6Ss during the initiation process. These novel findings illustrate how viral mRNA is threaded into the 40S subunit during the scanning process, exploiting the topology of the 40S subunit solvent side to enhance its translation in vertebrate hosts.

Indexed as

Peptide Chain Initiation, TranslationalAedesAlphavirusAnimalsBase SequenceCell LineCodon, InitiatorCricetinaeGene Expression Regulation, ViralInverted Repeat SequencesModels, MolecularRibosomesRNA, MessengerRNA, Ribosomal, 18SRNA StabilityRNA, ViralCodon, InitiatorRNA, MessengerRNA, Ribosomal, 18SRNA, Viral

Identifiers

PMID26984530
PMCPMC4872096
OpenAlexW2332390029

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.