Evidence map›Paper›PMID 19394297›Full record

ArticleMolecular cell2009

The plasticity of a translation arrest motif yields insights into nascent polypeptide recognition inside the ribosome tunnel.

Mee-Ngan Yap, Harris D Bernstein

Abstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

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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

64 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Cotranslational membrane insertion of the voltage-sensitive KProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
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  10. Article
  11. Article
  12. Article
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  14. Article
  15. Review
  16. Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Timing and specificity of cotranslational nascent protein modification in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. Article

4 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

2 authors.

Mee-Ngan YapGenetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Harris D Bernstein

Funding

Translational regulation in the ribosome tunnelZIADK052036 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BERNSTEIN, HARRIS · 2009 to 2013
$1.6M
Translational regulation in the ribosome tunnelZ01DK052036 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BERNSTEIN, HARRIS · 2007 to 2008
$906k
Intramural NIH HHS Z01 DK052036
6 · The paper itself

Abstract

The recognition of a C-terminal motif in E. coli SecM ((150)FXXXXWIXXXXGIRAGP(166)) inside the ribosome tunnel causes translation arrest, but the mechanism of recognition is unknown. Whereas single mutations in this motif impair recognition, we demonstrate that new arrest-inducing peptides can be created through remodeling of the SecM C terminus. We found that R163 is indispensable but that flanking residues that vary in number and position play an important secondary role in translation arrest. The observation that individual SecM variants showed a distinct pattern of crosslinking to ribosomal proteins suggests that each peptide adopts a unique conformation inside the tunnel. Based on the results, we propose that translation arrest occurs when the peptide conformation specified by flanking residues moves R163 into a precise intratunnel location. Our data indicate that translation arrest results from extensive communication between SecM and the tunnel and help to explain the striking diversity of arrest-inducing peptides found throughout nature.

Indexed as

Amino Acid MotifsAmino Acid SequenceEscherichia coliEscherichia coli ProteinsModels, GeneticMolecular Sequence DataMutationProtein BiosynthesisProtein Interaction MappingRibosomal ProteinsRibosomesSequence AlignmentTranscription FactorsEscherichia coli ProteinsRibosomal ProteinsSecM protein, E coliTranscription Factors

Identifiers

PMID19394297
PMCPMC2704006

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Registered trials

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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.