Evidence map›Paper›PMID 25143529›Full record

ArticleNucleic acids research2014

Translational stalling at polyproline stretches is modulated by the sequence context upstream of the stall site.

Agata L Starosta, Jürgen Lassak, Lauri Peil, Gemma C Atkinson, Kai Virumäe, Tanel Tenson, Jaanus Remme, Kirsten Jung, Daniel N Wilson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 100 citations in OpenAlex.

  1. Trial
  2. Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026
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  14. Tuning tRNAs for improved translation.Frontiers in genetics · 2024
    Review
  15. Article
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  17. Article
  18. Beyond antibiotic resistance: thebioRxiv : the preprint server for biology · 2023
    Article
  19. Article
  20. Article

10 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

9 authors at 3 institutions in 4 countries.

Agata L StarostaGene Center and Department for Biochemistry, University of Munich, Feodor-Lynenstr. 25, 81377 Munich, Germany.
Jürgen LassakDepartment of Biology I, Microbiology, Ludwig-Maximilians-Universität München, 82152 Martinsried, Germany.
Lauri PeilWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK Institute of Technology, University of Tartu, Tartu, Estonia.
Gemma C AtkinsonInstitute of Technology, University of Tartu, Tartu, Estonia Department of Molecular Biology and Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Umeå, Sweden.
Kai VirumäeInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Tanel TensonInstitute of Technology, University of Tartu, Tartu, Estonia.
Jaanus RemmeInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Kirsten JungDepartment of Biology I, Microbiology, Ludwig-Maximilians-Universität München, 82152 Martinsried, Germany Center for integrated Protein Science Munich (CiPSM) at the University of Munich, Munich, Germany.
Daniel N WilsonGene Center and Department for Biochemistry, University of Munich, Feodor-Lynenstr. 25, 81377 Munich, Germany Center for integrated Protein Science Munich (CiPSM) at the University of Munich, Munich, Germany wilson@genzentrum.lmu.de.
University of Tartu · EECenter for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The polymerization of amino acids into proteins occurs on ribosomes, with the rate influenced by the amino acids being polymerized. The imino acid proline is a poor donor and acceptor for peptide-bond formation, such that translational stalling occurs when three or more consecutive prolines (PPP) are encountered by the ribosome. In bacteria, stalling at PPP motifs is rescued by the elongation factor P (EF-P). Using SILAC mass spectrometry of Escherichia coli strains, we identified a subset of PPP-containing proteins for which the expression patterns remained unchanged or even appeared up-regulated in the absence of EF-P. Subsequent analysis using in vitro and in vivo reporter assays revealed that stalling at PPP motifs is influenced by the sequence context upstream of the stall site. Specifically, the presence of amino acids such as Cys and Thr preceding the stall site suppressed stalling at PPP motifs, whereas amino acids like Arg and His promoted stalling. In addition to providing fundamental insight into the mechanism of peptide-bond formation, our findings suggest how the sequence context of polyproline-containing proteins can be modulated to maximize the efficiency and yield of protein production.

Indexed as

PeptidesProtein BiosynthesisAmino Acid MotifsAmino AcidsAmino Acid SequenceEscherichia coliEscherichia coli ProteinsRibosomesUp-RegulationAmino AcidsEscherichia coli ProteinsPeptidespolyproline

Identifiers

PMID25143529
PMCPMC4176338
OpenAlexW2144773160

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.