Evidence map›Paper›PMID 18458056›Full record

ArticleMolecular and cellular biology2008

Site-specific release of nascent chains from ribosomes at a sense codon.

Victoria A Doronina, Cheng Wu, Pablo de Felipe, Matthew S Sachs, Martin D Ryan, Jeremy D Brown

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

100 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
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  7. Detailed phenotyping of Tbr1-2A-CreER knock-in mice demonstrates significant impacts on TBR1 protein levels and axon development.Autism research : official journal of the International Society for Autism Research · 2025
    Article
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  15. Review
  16. Article
  17. Synthetic polycistronic sequences in eukaryotes.Synthetic and systems biotechnology · 2021
    Review
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40 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

Victoria A DoroninaInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.
Cheng Wu
Pablo de Felipe
Matthew S Sachs
Martin D Ryan
Jeremy D Brown
Newcastle University · GBOregon Health & Science University · USUniversity of St Andrews · GB

Funding

CONTROL OF ARG-2 GENE EXPRESSION IN NEUROSPORAR01GM047498 · NIGMS · TEXAS A&M UNIVERSITY · PI SACHS, MATTHEW STEVEN · 1997 to 2009
$2.8M
CONTROL OF ARG-2 GENE EXPRESSION IN NEUROSPORAR29GM047498 · NIGMS · OREGON GRADUATE INSTITUTE SCIENCE &TECH · PI SACHS, MATTHEW S · 1992 to 1996
–
Biotechnology and Biological Sciences Research Council BB/E009093Biotechnology and Biological Sciences Research Council BB/E009093/1Biotechnology and Biological Sciences Research Council BB/E010709/1Biotechnology and Biological Sciences Research Council BB/E/01070911Biotechnology and Biological Sciences Research Council C20035Biotechnology and Biological Sciences Research Council C20418Medical Research Council G117/395NIGMS NIH HHS GM47498NIGMS NIH HHS R01 GM047498
6 · The paper itself

Abstract

"2A" oligopeptides are autonomous elements containing a D(V/I)EXNPGP motif at the C terminus. Protein synthesis from an open reading frame containing an internal 2A coding sequence yields two separate polypeptides, corresponding to sequences up to and including 2A and those downstream. We show that the 2A reaction occurs in the ribosomal peptidyltransferase center. Ribosomes pause at the end of the 2A coding sequence, over the glycine and proline codons, and the nascent chain up to and including this glycine is released. Translation-terminating release factors eRF1 and eRF3 play key roles in the reaction. On the depletion of eRF1, a greater proportion of ribosomes extend through the 2A coding sequence, yielding the full-length protein. In contrast, impaired eRF3 GTPase activity leads to many ribosomes failing to translate beyond 2A. Further, high-level expression of a 2A peptide-containing protein inhibits the growth of cells compromised for release factor activity and leads to errors in stop codon recognition. We propose that the nascent 2A peptide interacts with ribosomes to drive a highly unusual and specific "termination" reaction, despite the presence of a proline codon in the A site. After this, the majority of ribosomes continue translation, generating the separate downstream product.

Indexed as

Amino Acid SequenceAnimalsCattleCodonMiceModels, BiologicalMolecular Sequence DataOpen Reading FramesPeptidesPeptide Termination FactorsProtein BiosynthesisRibosomesRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCodonPeptidesPeptide Termination FactorsRNA, Transfer, Amino AcylSaccharomyces cerevisiae ProteinstRNA, peptidyl-

Identifiers

PMID18458056
PMCPMC2447138
OpenAlexW2130286786

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.