Evidence map›Paper›PMID 39622818›Full record

ArticleNature communications2024

EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.

Alina Sieber, Marina Parr, Julian von Ehr, Karthikeyan Dhamotharan, Pavel Kielkowski, Tess Brewer, Anna Schäpers, Ralph Krafczyk, Fei Qi, Andreas Schlundt and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

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

7 citing papers in PubMed.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Pleiotropic roles of elongation factor P inMicrobiology spectrum · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. 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

12 authors.

Alina Sieber *Faculty of Biology, Microbiology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.ORCID 0000-0003-3910-6868
Marina Parr *Department of Bioinformatics, Wissenschaftszentrum Weihenstephan, Technische Universität München, Freising, Germany.ORCID 0000-0003-3182-6713
Julian von EhrInstitute for Molecular Biosciences and Biomolecular Resonance Center (BMRZ), Goethe University Frankfurt, Frankfurt, Germany.ORCID 0000-0003-4535-661X
Karthikeyan DhamotharanInstitute for Molecular Biosciences and Biomolecular Resonance Center (BMRZ), Goethe University Frankfurt, Frankfurt, Germany.ORCID 0000-0003-0226-7350
Pavel KielkowskiDepartment of Chemistry, Institut für Chemische Epigenetik (ICEM), Ludwig-Maximilians-Universität München, Munich, Germany.ORCID 0000-0003-4910-6263
Tess BrewerFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.ORCID 0000-0001-7855-5610
Anna SchäpersFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
Ralph KrafczykFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.ORCID 0000-0001-6171-6086
Fei QiState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen, China.ORCID 0000-0003-4578-0146
Andreas SchlundtInstitute for Molecular Biosciences and Biomolecular Resonance Center (BMRZ), Goethe University Frankfurt, Frankfurt, Germany.ORCID 0000-0003-2254-7560
Dmitrij FrishmanDepartment of Bioinformatics, Wissenschaftszentrum Weihenstephan, Technische Universität München, Freising, Germany.ORCID 0000-0001-7744-9402
Jürgen LassakFaculty of Biology, Microbiology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany. juergen.lassak@lmu.de.ORCID 0000-0003-3936-3389

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) LA 3658/5-1Deutsche Forschungsgemeinschaft (German Research Foundation) SCHL2062/2-2Verband der Chemischen Industrie (Chemical Industry Association) Liebig Fellowship
6 · The paper itself

Abstract

Polyproline sequences are deleterious to cells because they stall ribosomes. In bacteria, EF-P plays an important role in overcoming such polyproline sequence-induced ribosome stalling. Additionally, numerous bacteria possess an EF-P paralog called EfpL (also known as YeiP) of unknown function. Here, we functionally and structurally characterize EfpL from Escherichia coli and demonstrate its role in the translational stress response. Through ribosome profiling, we analyze the EfpL arrest motif spectrum and find additional sequences beyond the canonical polyproline motifs that both EF-P and EfpL can resolve. Notably, the two factors can also induce pauses. We further report that EfpL can sense the metabolic state of the cell via lysine acylation. Overall, our work characterizes the role of EfpL in ribosome rescue at proline-containing sequences, and provides evidence that co-occurrence of EF-P and EfpL is an evolutionary driver for higher bacterial growth rates.

Indexed as

Escherichia coliEscherichia coli ProteinsPeptide Elongation FactorsProlineProtein BiosynthesisRibosomesAcylationLysinePeptidesEscherichia coli Proteinsfactor EF-PLysinePeptide Elongation FactorsPeptidespolyprolineProline

Identifiers

PMID39622818
PMCPMC11611912

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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.