Evidence map›Paper›PMID 27257056›Full record

ArticleNucleic acids research2016

A novel role for poly(C) binding proteins in programmed ribosomal frameshifting.

Sawsan Napthine, Emmely E Treffers, Susanne Bell, Ian Goodfellow, Ying Fang, Andrew E Firth, Eric J Snijder, Ian Brierley

Abstract 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 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Nontriplet feature of genetic code inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Classification, replication, and transcription ofFrontiers in microbiology · 2023
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  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

8 authors.

Sawsan NapthineDepartment of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK.
Emmely E TreffersDepartment of Medical Microbiology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands.
Susanne BellDepartment of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK.
Ian GoodfellowDepartment of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK.
Ying FangCollege of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-5705, USA.
Andrew E FirthDepartment of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK aef24@cam.ac.uk.
Eric J SnijderDepartment of Medical Microbiology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands e.j.snijder@lumc.nl.
Ian BrierleyDepartment of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK ib103@mole.bio.cam.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/L000334/1Wellcome Trust 088789Wellcome Trust 097997/Z/11/ZWellcome Trust 106207
6 · The paper itself

Abstract

Translational control through programmed ribosomal frameshifting (PRF) is exploited widely by viruses and increasingly documented in cellular genes. Frameshifting is induced by mRNA secondary structures that compromise ribosome fidelity during decoding of a heptanucleotide 'slippery' sequence. The nsp2 PRF signal of porcine reproductive and respiratory syndrome virus is distinctive in directing both -2 and -1 PRF and in its requirement for a trans-acting protein factor, the viral replicase subunit nsp1β. Here we show that the the trans-activation of frameshifting is carried out by a protein complex composed of nsp1β and a cellular poly(C) binding protein (PCBP). From the results of in vitro translation and electrophoretic mobility shift assays, we demonstrate that a PCBP/nsp1β complex binds to a C-rich sequence downstream of the slippery sequence and here mimics the activity of a structured mRNA stimulator of PRF. This is the first description of a role for a trans-acting cellular protein in PRF. The discovery broadens the repertoire of activities associated with poly(C) binding proteins and prototypes a new class of virus-host interactions.

Indexed as

AnimalsBase SequenceCysteine EndopeptidasesFrameshifting, RibosomalMultiprotein ComplexesNucleic Acid ConformationPorcine respiratory and reproductive syndrome virusProtein BiosynthesisRibosomesRNA-Binding ProteinsRNA, MessengerSwineCysteine EndopeptidasesMultiprotein ComplexesnsP2 proteinaseRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID27257056
PMCPMC4937337

What OpenQuestion holds

Textmetadata
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.