Evidence map›Paper›PMID 35609997›Full record

ArticleNucleic acids research2022

GNAT toxins evolve toward narrow tRNA target specificities.

Dmitry Bikmetov, Alexander M J Hall, Alexei Livenskyi, Bridget Gollan, Stepan Ovchinnikov, Konstantin Gilep, Jenny Y Kim, Gerald Larrouy-Maumus, Viktor Zgoda, Sergei Borukhov and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Specificity and mechanism of tRNA cleavage by the AriB Toprim nuclease of the PARIS bacterial immune system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  3. Article
  4. 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

13 authors at 8 institutions in 3 countries.

Dmitry BikmetovCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Alexander M J HallDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.
Alexei LivenskyiCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Bridget GollanDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.
Stepan OvchinnikovCenter for Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo 143025, Russia.
Konstantin GilepCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences, Moscow 119334, Russia.
Jenny Y KimDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.
Gerald Larrouy-MaumusMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Viktor ZgodaInstitute of Biomedical Chemistry, Moscow 119435, Russia.
Sergei BorukhovDepartment of Cell Biology and Neuroscience, Rowan University School of Osteopathic Medicine, Stratford, NJ 08084-1489, USA.
Konstantin SeverinovInstitute of Molecular Genetics of National Research Center «Kurchatov Institute», Moscow 123182, Russia.ORCID 0000-0001-9706-450X
Sophie HelaineDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.
Svetlana DubileyCenter for Life Sciences, Skolkovo Institute of Science and Technology, Skolkovo 143025, Russia.
Harvard University · USSkolkovo Institute of Science and Technology · RUImperial College London · GBInstitute of Biomedical Chemistry · RUInstitute of Gene Biology · RUKurchatov Institute · RULomonosov Moscow State University · RURowan University · US

Funding

The physiological activation and consequences of Toxin-Antitoxin systems in SalmonellaR01AI155552 · NIAID · HARVARD MEDICAL SCHOOL · PI HELAINE, SOPHIE · 2021 to 2025
$2.5M
NIAID NIH HHS R01 AI155552
6 · The paper itself

Abstract

Type II toxin-antitoxin (TA) systems are two-gene modules widely distributed among prokaryotes. GNAT toxins associated with the DUF1778 antitoxins represent a large family of type II TAs. GNAT toxins inhibit cell growth by disrupting translation via acetylation of aminoacyl-tRNAs. In this work, we explored the evolutionary trajectory of GNAT toxins. Using LC/MS detection of acetylated aminoacyl-tRNAs combined with ribosome profiling, we systematically investigated the in vivo substrate specificity of an array of diverse GNAT toxins. Our functional data show that the majority of GNAT toxins are specific to Gly-tRNA isoacceptors. However, the phylogenetic analysis shows that the ancestor of GNAT toxins was likely a relaxed specificity enzyme capable of acetylating multiple elongator tRNAs. Together, our data provide a remarkable snapshot of the evolution of substrate specificity.

Indexed as

AntitoxinsBacterial ToxinsToxin-Antitoxin SystemsBacterial ProteinsPhylogenyRNA, TransferRNA, Transfer, Amino AcylAntitoxinsBacterial ProteinsBacterial ToxinsRNA, TransferRNA, Transfer, Amino Acyl

Identifiers

PMID35609997
PMCPMC9177977
OpenAlexW4282923235

What OpenQuestion holds

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LicenceCC BY
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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.