Evidence map›Paper›PMID 35638832›Full record

ArticleMicrobiology spectrum2022

A tRNA-Acetylating Toxin and Detoxifying Enzyme in Mycobacterium tuberculosis.

Francesca G Tomasi, Alexander M J Hall, Jessica T P Schweber, Charles L Dulberger, Kerry McGowen, Qingyun Liu, Sarah M Fortune, Sophie Helaine, Eric J Rubin

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Development of a Potent and FunctionalJournal of medicinal chemistry · 2025
    Article
  2. Are all VapC toxins ofJournal of biosciences · 2024
    Article
  3. Article
  4. Article
  5. The role ofFrontiers in cellular and infection microbiology · 2023
    Review
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

9 authors at 1 institution in 1 country.

Francesca G TomasiDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.ORCID 0000-0003-1421-9284
Alexander M J HallDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts, USA.
Jessica T P SchweberDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.
Charles L DulbergerDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.
Kerry McGowenDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.
Qingyun LiuDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.
Sarah M FortuneDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.ORCID 0000-0001-7565-9975
Sophie HelaineDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts, USA.
Eric J RubinDepartment of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.ORCID 0000-0001-5120-962X
Harvard University · US

Funding

Vulnerabilities in Mycobacterial Cell-Wall BiogenesisP01AI095208 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI SACCHETTINI, JAMES C · 2012 to 2022
$19.8M
NIAID NIH HHS P01 AI095208
6 · The paper itself

Abstract

Toxin-antitoxin (TA) systems allow bacteria to adapt to changing environments without altering gene expression. Despite being overrepresented in Mycobacterium tuberculosis, their physiological roles remain elusive. We describe a TA system in M. tuberculosis which we named TacAT due to its homology to previously discovered systems in Salmonella. The toxin, TacT, blocks growth by acetylating glycyl-tRNAs and inhibiting translation. Its effects are reversed by the enzyme peptidyl tRNA hydrolase (Pth), which also cleaves peptidyl tRNAs that are prematurely released from stalled ribosomes. Pth is essential in most bacteria and thereby has been proposed as a promising drug target for complex pathogens like M. tuberculosis. Transposon sequencing data suggest that the

Indexed as

AntitoxinsBacterial ToxinsMycobacterium tuberculosisTuberculosisAnti-Bacterial AgentsBacterial ProteinsHumansRNA, TransferAnti-Bacterial AgentsAntitoxinsBacterial ProteinsBacterial ToxinsRNA, Transferantibiotic resistanceMycobacterium tuberculosistoxin/antitoxin systemstranslationtRNA modification

Identifiers

PMID35638832
PMCPMC9241777
OpenAlexW4282930665

What OpenQuestion holds

Textmetadata
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.