Evidence map›Paper›PMID 26740583›Full record

ArticleNucleic acids research2016

tRNA is a new target for cleavage by a MazF toxin.

Jason M Schifano, Jonathan W Cruz, Irina O Vvedenskaya, Regina Edifor, Ming Ouyang, Robert N Husson, Bryce E Nickels, Nancy A Woychik

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Identification of Genes Encoded Toxin-Antitoxin System inInfectious disorders drug targets · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Article
  19. Review
  20. Conserved Amino Acid Moieties ofFrontiers in microbiology · 2021
    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 3 institutions in 1 country.

Jason M SchifanoDepartment of Biochemistry and Molecular Biology, Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ, USA.ORCID http://orcid.org/0000-0002-8072-9613
Jonathan W CruzDepartment of Biochemistry and Molecular Biology, Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ, USA.
Irina O VvedenskayaWaksman Institute, Rutgers University, Piscataway, NJ, USA Department of Genetics, Rutgers University, Piscataway, NJ, USA.
Regina EdiforDivision of Infectious Diseases, Boston Children's Hospital/Harvard Medical School, Boston, MA, USA.
Ming OuyangDepartment of Computer Science, University of Massachusetts Boston, Boston, MA, USA.
Robert N HussonDivision of Infectious Diseases, Boston Children's Hospital/Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0001-8994-7046
Bryce E NickelsWaksman Institute, Rutgers University, Piscataway, NJ, USA Department of Genetics, Rutgers University, Piscataway, NJ, USA Member, Rutgers Cancer Institute of New Jersey, NJ, USA.
Nancy A WoychikDepartment of Biochemistry and Molecular Biology, Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ, USA Member, Rutgers Cancer Institute of New Jersey, NJ, USA nancy.woychik@rutgers.edu.
Rutgers, The State University of New Jersey · USBoston Children's Hospital · USUniversity of Massachusetts Boston · US

Funding

NanoRNA-mediated control of gene expressionR01GM096454 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI DOVE, SIMON L, NICKELS, BRYCE EDWARD · 2010 to 2014
$3.7M
VIRUS-HOST INTERACTIONS IN EUKARYOTIC CELLST32AI007403 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI BREWER, GARY A. · 1991 to 2014
$1.7M
In Vivo Studies of Abortive InitiationR01GM088343 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI NICKELS, BRYCE EDWARD · 2011 to 2015
$1.7M
Membrane Protein Production Using the Yeast SPP SystemR01GM095693 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI WOYCHIK, NANCY ANN · 2010 to 2013
$1.3M
M. tuberculosis MazF toxins: target identification and stress adaptationR56AI119055 · NIAID · RBHS-ROBERT WOOD JOHNSON MEDICAL SCHOOL · PI WOYCHIK, NANCY ANN · 2015 to 2015
$549k
Functional Dissection of Toxin-Antitoxin Systems in Mycobacterium tuberculosisR21AI072399 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI WOYCHIK, NANCY ANN · 2009 to 2010
$463k
NIAID NIH HHS R21 AI072399NIAID NIH HHS R56 AI119055NIAID NIH HHS T32AI007403NIGMS NIH HHS GM096454NIGMS NIH HHS R01 GM088343NIGMS NIH HHS R01 GM095693
6 · The paper itself

Abstract

Toxin-antitoxin (TA) systems play key roles in bacterial persistence, biofilm formation and stress responses. The MazF toxin from the Escherichia coli mazEF TA system is a sequence- and single-strand-specific endoribonuclease, and many studies have led to the proposal that MazF family members exclusively target mRNA. However, recent data indicate some MazF toxins can cleave specific sites within rRNA in concert with mRNA. In this report, we identified the repertoire of RNAs cleaved by Mycobacterium tuberculosis toxin MazF-mt9 using an RNA-seq-based approach. This analysis revealed that two tRNAs were the principal targets of MazF-mt9, and each was cleaved at a single site in either the tRNA(Pro14) D-loop or within the tRNA(Lys43) anticodon. This highly selective target discrimination occurs through recognition of not only sequence but also structural determinants. Thus, MazF-mt9 represents the only MazF family member known to target tRNA and to require RNA structure for recognition and cleavage. Interestingly, the tRNase activity of MazF-mt9 mirrors basic features of eukaryotic tRNases that also generate stable tRNA-derived fragments that can inhibit translation in response to stress. Our data also suggest a role for tRNA distinct from its canonical adapter function in translation, as cleavage of tRNAs by MazF-mt9 downregulates bacterial growth.

Indexed as

AnticodonBacterial ProteinsBase SequenceBinding SitesBlotting, NorthernEndoribonucleasesModels, MolecularMycobacterium tuberculosisNucleic Acid ConformationProtein BindingRNA, BacterialRNA, TransferAnticodonBacterial ProteinsEndoribonucleasesMazF protein, Mycobacterium tuberculosisRNA, BacterialRNA, Transfer

Identifiers

PMID26740583
PMCPMC4756823
OpenAlexW2229297191

What OpenQuestion holds

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LicenceCC BY-NC
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.