Evidence map›Paper›PMID 39903774›Full record

ArticlePLoS genetics2025

D-stem mutation in an essential tRNA increases translation speed at the cost of fidelity.

Madison N Schrock, Krishna Parsawar, Kelly T Hughes, Fabienne F V Chevance

Abstract read
In one paragraph

Article in PLoS genetics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. 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

4 authors.

Madison N SchrockSchool of Biological Sciences, University of Utah, Salt Lake City, Utah, United States of America.ORCID https://orcid.org/0000-0001-7946-8615
Krishna ParsawarAnalytical and Biological Mass Spectrometry Core, University of Arizona, Tucson, Arizona, United States of America.ORCID https://orcid.org/0009-0001-2325-7621
Kelly T HughesSchool of Biological Sciences, University of Utah, Salt Lake City, Utah, United States of America.ORCID https://orcid.org/0000-0001-5344-0972
Fabienne F V ChevanceSchool of Biological Sciences, University of Utah, Salt Lake City, Utah, United States of America.ORCID https://orcid.org/0000-0003-2997-3466

Funding

Coupling gene regulation to flagellar morphogenesisR01GM056141 · NIGMS · UNIVERSITY OF WASHINGTON · PI HUGHES, KELLY T · 1998 to 2023
$8.3M
Salmonella type III secretion: substrate targeting and injectisome assemblyR56AI184395 · NIAID · UNIVERSITY OF UTAH · PI HUGHES, KELLY T · 2024 to 2024
$728k
NIAID NIH HHS R56 AI184395NIGMS NIH HHS R01 GM056141
6 · The paper itself

Abstract

The efficiency with which aminoacyl-tRNA and GTP-bound translation elongation factor EF-Tu recognizes the A-site codon of the ribosome is dependent on codons and tRNA species present in the polypeptide (P) and exit (E) codon sites. To understand how codon context affects the efficiency of codon recognition by tRNA-bound EF-Tu, a genetic system was developed to select for fast translation through slow-translating codon combinations. Selection for fast translation through the slow-translated UCA-UAC pair, flanked by histidine codons, resulted in the isolation of an A25G base substitution mutant in the D-stem of an essential tRNA LeuZ, which recognizes the UUA and UUG leucine codons. The LeuZ(A25G) substitution allowed for faster translation through all codon pairs tested that included the UCA codon. Insertion of leucine at the UCA serine codon was enhanced in the presence of LeuZ(A25G) tRNA. This work, taken in context with the Hirsh UGA nonsense suppressor G24A mutation in TrpT tRNA, provides genetic evidence that the post-GTP hydrolysis proofreading step by elongation factor Tu may be controlled by structural interactions in the hinge region of tRNA species. Our results support a model in which the tRNA bending component of the accommodation step in mRNA translation allows EF Tu time to enhance its ability to differentiate tRNA interactions between cognate and near-cognate mRNA codons.

Indexed as

Peptide Elongation Factor TuProtein BiosynthesisRNA, TransferRNA, Transfer, LeuCodonGuanosine TriphosphateMutationRibosomesCodonGuanosine TriphosphatePeptide Elongation Factor TuRNA, TransferRNA, Transfer, Leu

Identifiers

PMID39903774
PMCPMC11805395

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Registered trials

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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.