Evidence map›Paper›PMID 29389943›Full record

ArticlePLoS computational biology2018

Evolutionary analysis of polyproline motifs in Escherichia coli reveals their regulatory role in translation.

Fei Qi, Magdalena Motz, Kirsten Jung, Jürgen Lassak, Dmitrij Frishman

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-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

24 citing papers in PubMed, 40 citations in OpenAlex.

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  18. Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020
    Review
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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

5 authors at 3 institutions in 2 countries.

Fei QiDepartment of Bioinformatics, Wissenschaftzentrum Weihenstephan, Technische Universität München, Freising, Germany.ORCID 0000-0003-4578-0146
Magdalena MotzCenter for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Munich, Germany.
Kirsten JungCenter for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0003-0779-6841
Jürgen LassakCenter for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0003-3936-3389
Dmitrij FrishmanDepartment of Bioinformatics, Wissenschaftzentrum Weihenstephan, Technische Universität München, Freising, Germany.
Center for Integrated Protein Science Munich · DEPeter the Great St. Petersburg Polytechnic University · RUWeihenstephan-Triesdorf University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translation of consecutive prolines causes ribosome stalling, which is alleviated but cannot be fully compensated by the elongation factor P. However, the presence of polyproline motifs in about one third of the E. coli proteins underlines their potential functional importance, which remains largely unexplored. We conducted an evolutionary analysis of polyproline motifs in the proteomes of 43 E. coli strains and found evidence of evolutionary selection against translational stalling, which is especially pronounced in proteins with high translational efficiency. Against the overall trend of polyproline motif loss in evolution, we observed their enrichment in the vicinity of translational start sites, in the inter-domain regions of multi-domain proteins, and downstream of transmembrane helices. Our analysis demonstrates that the time gain caused by ribosome pausing at polyproline motifs might be advantageous in protein regions bracketing domains and transmembrane helices. Polyproline motifs might therefore be crucial for co-translational folding and membrane insertion.

Indexed as

Amino Acid MotifsPeptide Chain Elongation, TranslationalProtein BiosynthesisEscherichia coliEscherichia coli ProteinsEvolution, MolecularPeptide Elongation FactorsPeptidesPhylogenyProtein FoldingProteomeProteomicsRibosomesEscherichia coli Proteinsfactor EF-PPeptide Elongation FactorsPeptidespolyprolineProteome

Identifiers

PMID29389943
PMCPMC5811046
OpenAlexW2785449688

What OpenQuestion holds

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LicenceCC BY
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.