Evidence map›Paper›PMID 31114007›Full record

ArticleScientific reports2019

Identification and first characterization of DinJ-YafQ toxin-antitoxin systems in Lactobacillus species of biotechnological interest.

Alberto Ferrari, Stefano Maggi, Barbara Montanini, Alessia Levante, Camilla Lazzi, Yoshihiro Yamaguchi, Claudio Rivetti, Claudia Folli

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Identification of Type II Toxin-Antitoxin Loci in Levilactobacillus brevis.Interdisciplinary sciences, computational life sciences · 2022
    Article
  5. Article
  6. Article
  7. Genome Sequencing of fiveMicroorganisms · 2021
    Article
  8. Article
  9. Expression of DinJ-YafQ System ofMicroorganisms · 2019
    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

8 authors at 2 institutions in 2 countries.

Alberto FerrariDepartment of Food and Drug, University of Parma, 43124, Parma, Italy.
Stefano MaggiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124, Parma, Italy.
Barbara MontaniniDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124, Parma, Italy.ORCID http://orcid.org/0000-0002-5419-7975
Alessia LevanteDepartment of Food and Drug, University of Parma, 43124, Parma, Italy.
Camilla LazziDepartment of Food and Drug, University of Parma, 43124, Parma, Italy.
Yoshihiro YamaguchiThe OCU Advanced Research Institute for Natural Science and Technology (OCARINA), Osaka City University, Sumiyoshi-ku, 558-8585, Osaka, Japan.
Claudio RivettiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124, Parma, Italy. claudio.rivetti@unipr.it.
Claudia FolliDepartment of Food and Drug, University of Parma, 43124, Parma, Italy. claudia.folli@unipr.it.
University of Parma · ITOsaka City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DinJ-YafQ is a type II TA system comprising the ribosome-dependent RNase YafQ toxin and the DinJ antitoxin protein. Although the module has been extensively characterized in Escherichia coli, little information is available for homologous systems in lactic acid bacteria. In this study, we employed bioinformatics tools to identify DinJ-YafQ systems in Lactobacillus casei, Lactobacillus paracasei and Lactobacillus rhamnosus species, commonly used in biotechnological processes. Among a total of nineteen systems found, two TA modules from Lactobacillus paracasei and two modules from Lactobacillus rhamnosus wild strains were isolated and their activity was verified by growth assays in Escherichia coli either in liquid and solid media. The RNase activity of the YafQ toxins was verified in vivo by probing mRNA dynamics and metabolism with single-cell Thioflavin T fluorescence. Our findings demonstrate that, albeit DinJ-YafQ TA systems are widely distributed in lactic acid bacteria, only few are fully functional, while others have lost toxicity even though they maintain high sequence identity with wild type YafQ and a likely functional antitoxin protein.

Indexed as

Bacterial ToxinsBinding SitesLactobacillusPhylogenyProtein BindingBacterial Toxins

Identifiers

PMID31114007
PMCPMC6529426
OpenAlexW2945851067

What OpenQuestion holds

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LicenceCC BY
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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.