Evidence map›Paper›PMID 27377007›Full record

ArticleScientific reports2016

Proteome-wide measurement of non-canonical bacterial mistranslation by quantitative mass spectrometry of protein modifications.

Nevena Cvetesic, Maja Semanjski, Boumediene Soufi, Karsten Krug, Ita Gruic-Sovulj, Boris Macek

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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  6. Review
  7. Article
  8. Exploiting evolutionary trade-offs for posttreatment management of drug-resistant populations.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Loss of protein synthesis quality control in host-restricted organisms.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Review
  13. MS-READ: Quantitative measurement of amino acid incorporation.Biochimica et biophysica acta. General subjects · 2017
    Article
  14. Article
  15. Mass spectrometric identification of phenol-soluble modulins in the ATCC® 43300 standard strain of methicillin-resistant Staphylococcus aureus harboring two distinct phenotypes.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2017
    Article
  16. 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

6 authors at 2 institutions in 2 countries.

Nevena CvetesicChemistry Department, Faculty of Science, University of Zagreb, Croatia.
Maja SemanjskiProteome Center Tuebingen, University of Tuebingen, Germany.
Boumediene SoufiProteome Center Tuebingen, University of Tuebingen, Germany.
Karsten KrugProteome Center Tuebingen, University of Tuebingen, Germany.
Ita Gruic-SovuljChemistry Department, Faculty of Science, University of Zagreb, Croatia.
Boris MacekProteome Center Tuebingen, University of Tuebingen, Germany.
University of Tübingen · DEUniversity of Zagreb · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genetic code is virtually universal in biology and was likely established before the advent of cellular life. The extent to which mistranslation occurs is poorly understood and presents a fundamental question in basic research and production of recombinant proteins. Here we used shotgun proteomics combined with unbiased protein modification analysis to quantitatively analyze in vivo mistranslation in an E. coli strain with a defect in the editing mechanism of leucyl-tRNA synthetase. We detected the misincorporation of a non-proteinogenic amino acid norvaline on 10% of all measured leucine residues under microaerobic conditions and revealed preferential deployment of a tRNA(Leu)(CAG) isoacceptor during norvaline misincorporation. The strain with the norvalylated proteome demonstrated a substantial reduction in cell fitness under both prolonged aerobic and microaerobic cultivation. Unlike norvaline, isoleucine did not substitute for leucine even under harsh error-prone conditions. Our study introduces shotgun proteomics as a powerful tool in quantitative analysis of mistranslation.

Indexed as

Escherichia coliProtein BiosynthesisProtein Processing, Post-TranslationalProteomeMass SpectrometryProteome

Identifiers

PMID27377007
PMCPMC4932531
OpenAlexW2472990078

What OpenQuestion holds

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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.