Evidence map›Paper›PMID 40193707›Full record

ArticleNucleic acids research2025

Altering translation allows E. coli to overcome G-quadruplex stabilizers.

Rachel R Cueny, Andrew F Voter, Aidan M McKenzie, Marcel Morgenstern, Kevin S Myers, Michael M Place, Jason M Peters, Joshua J Coon, James L Keck

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Rachel R CuenyBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706 United States.ORCID 0000-0002-7388-6864
Andrew F VoterBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706 United States.
Aidan M McKenzieBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706 United States.
Marcel MorgensternBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706 United States.
Kevin S MyersGreat Lakes Bioenergy Research Center and the Wisconsin Energy Institute, University of Wisconsin-Madison, Madison, WI, 53726 United States.ORCID 0000-0003-3302-3877
Michael M PlaceGreat Lakes Bioenergy Research Center and the Wisconsin Energy Institute, University of Wisconsin-Madison, Madison, WI, 53726 United States.
Jason M PetersPharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, Madison, WI, 53706 United States.
Joshua J CoonBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706 United States.
James L KeckBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706 United States.ORCID 0000-0002-5961-0220

Funding

TR&D 2 Metabolic Labels for Ultraplexed Protein Quantification p. 453P41GM108538 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$13.1M
Structure, Function and Regulation of the ProteomeR35GM118110 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$9.1M
Structure and Function of the Bacterial PrimosomeR01GM098885 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI James L Keck · 2012 to 2026
$4.0M
The critical roles of (p)ppGpp in homeostasis and antibiotic tolerance in Gram positive bacteriaR35GM127088 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Jue D. Wang · 2018 to 2026
$3.9M
NIGMS NIH HHS P41 GM108538NIGMS NIH HHS R01 GM098885NIGMS NIH HHS R01GM098885NIGMS NIH HHS R35 GM118110NIGMS NIH HHS R35 GM127088
6 · The paper itself

Abstract

G-quadruplex (G4) structures can form in guanine-rich DNA or RNA and have been found to modulate cellular processes, including replication, transcription, and translation. Many studies on the cellular roles of G4s have focused on eukaryotic systems, with far fewer probing bacterial G4s. Using a chemical-genetic approach, we identified genes in Escherichia coli that are important for growth in G4-stabilizing conditions. Reducing levels of translation elongation factor Tu or slowing translation initiation or elongation with kasugamycin, chloramphenicol, or spectinomycin suppress the effects of G4-stabilizing compounds. In contrast, reducing the expression of specific translation termination or ribosome recycling proteins is detrimental to growth in G4-stabilizing conditions. Proteomic and transcriptomic analyses reveal decreased protein and transcript levels, respectively, for ribosome assembly factors and proteins associated with translation in the presence of G4 stabilizer. Our results support a model in which reducing the rate of translation by altering translation initiation, translation elongation, or ribosome assembly can compensate for G4-related stress in E. coli.

Indexed as

DNA, BacterialDNA Transposable ElementsEscherichia coliG-QuadruplexesCRISPR-Cas SystemsEscherichia coli ProteinsGene DeletionGene Expression Regulation, BacterialPeptide Elongation Factor TuProtein BiosynthesisProteomicsRibosomesDNA, BacterialDNA Transposable ElementsEscherichia coli ProteinsPeptide Elongation Factor TutufB protein, E coli

Identifiers

PMID40193707
PMCPMC11975287

What OpenQuestion holds

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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.