Evidence map›Paper›PMID 24919156›Full record

ArticleNature2014

Dynamic pathways of -1 translational frameshifting.

Jin Chen, Alexey Petrov, Magnus Johansson, Albert Tsai, Seán E O'Leary, Joseph D Puglisi

Abstract read
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
8.3field-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

121 citing papers in PubMed, 170 citations in OpenAlex.

  1. Recoding by NNature communications · 2026
    Article
  2. Article
  3. tRNA modifications in viral replication.The Journal of biological chemistry · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Ribosome-induced mRNA pseudoknot interactions visualized by DMS MaP-Seq.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Conserved 5-methyluridine tRNA modification modulates ribosome translocation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Phenotypic mutations contribute to protein diversity and shape protein evolution.Protein science : a publication of the Protein Society · 2022
    Review
  19. Review
  20. Article

61 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 1 institution in 1 country.

Jin Chen1] Department of Applied Physics, Stanford University, Stanford, California 94305-4090, USA [2] Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Alexey PetrovDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Magnus JohanssonDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Albert Tsai1] Department of Applied Physics, Stanford University, Stanford, California 94305-4090, USA [2] Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Seán E O'LearyDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California 94305-5126, USA.
Stanford University · US

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
Single molecule translational profilingR01GM099687 · NIGMS · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D · 2011 to 2015
$4.3M
NIGMS NIH HHS GM099687NIGMS NIH HHS GM51266NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM099687
6 · The paper itself

Abstract

Spontaneous changes in the reading frame of translation are rare (frequency of 10(-3) to 10(-4) per codon), but can be induced by specific features in the messenger RNA (mRNA). In the presence of mRNA secondary structures, a heptanucleotide 'slippery sequence' usually defined by the motif X XXY YYZ, and (in some prokaryotic cases) mRNA sequences that base pair with the 3' end of the 16S ribosomal rRNA (internal Shine-Dalgarno sequences), there is an increased probability that a specific programmed change of frame occurs, wherein the ribosome shifts one nucleotide backwards into an overlapping reading frame (-1 frame) and continues by translating a new sequence of amino acids. Despite extensive biochemical and genetic studies, there is no clear mechanistic description for frameshifting. Here we apply single-molecule fluorescence to track the compositional and conformational dynamics of individual ribosomes at each codon during translation of a frameshift-inducing mRNA from the dnaX gene in Escherichia coli. Ribosomes that frameshift into the -1 frame are characterized by a tenfold longer pause in elongation compared to non-frameshifted ribosomes, which translate through unperturbed. During the pause, interactions of the ribosome with the mRNA stimulatory elements uncouple EF-G catalysed translocation from normal ribosomal subunit reverse-rotation, leaving the ribosome in a non-canonical intersubunit rotated state with an exposed codon in the aminoacyl-tRNA site (A site). tRNA(Lys) sampling and accommodation to the empty A site and EF-G action either leads to the slippage of the tRNAs into the -1 frame or maintains the ribosome into the 0 frame. Our results provide a general mechanistic and conformational framework for -1 frameshifting, highlighting multiple kinetic branchpoints during elongation.

Indexed as

Frameshifting, RibosomalPeptide Chain Elongation, TranslationalBacterial ProteinsCodonDNA Polymerase IIIEscherichia coliKineticsPeptide Elongation Factor GReading FramesRibosomesRibosome SubunitsRNA, MessengerRNA, Transfer, Amino AcylRotationTime FactorsBacterial ProteinsCodonDNA Polymerase IIIDnaX protein, BacteriaPeptide Elongation Factor GRNA, MessengerRNA, Transfer, Amino Acyl

Identifiers

PMID24919156
PMCPMC4472451
OpenAlexW2033946310

What OpenQuestion holds

Textmetadata
LicenceTDM
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.