Evidence map›Paper›PMID 24748661›Full record

ArticleNucleic acids research2014

RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system in Escherichia coli.

Yunxue Guo, Cecilia Quiroga, Qin Chen, Michael J McAnulty, Michael J Benedik, Thomas K Wood, Xiaoxue Wang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

67 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Toxins · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Unveil the Secret of the Bacteria and Phage Arms Race.International journal of molecular sciences · 2023
    Review
  20. Review

7 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Yunxue GuoKey Laboratory of Tropical Marine Bio-resources and Ecology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, PR China.
Cecilia QuirogaDepartment of Chemical Engineering, Pennsylvania State University, University Park, PA 16802-4400, USA.
Qin ChenDepartment of Chemical Engineering, Pennsylvania State University, University Park, PA 16802-4400, USA.
Michael J McAnultyDepartment of Chemical Engineering, Pennsylvania State University, University Park, PA 16802-4400, USA.
Michael J BenedikDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802-4400, USA.
Thomas K WoodDepartment of Chemical Engineering, Pennsylvania State University, University Park, PA 16802-4400, USA Department of Biology, Texas A & M University, College Station, TX 77843-3258, USA xxwang@scsio.ac.cn.
Xiaoxue WangKey Laboratory of Tropical Marine Bio-resources and Ecology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, PR China xxwang@scsio.ac.cn.
Pennsylvania State University · USInstitute of Oceanology · CNTexas A&M University · US

Funding

Re-Wiring Cellular Metabolism to Control Biofilm Formation and Virulence BY...R01GM089999 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI WOOD, THOMAS K · 2009 to 2011
$846k
NIGMS NIH HHS R01 GM089999
6 · The paper itself

Abstract

For toxin/antitoxin (TA) systems, no toxin has been identified that functions by cleaving DNA. Here, we demonstrate that RalR and RalA of the cryptic prophage rac form a type I TA pair in which the antitoxin RNA is a trans-encoded small RNA with 16 nucleotides of complementarity to the toxin mRNA. We suggest the newly discovered antitoxin gene be named ralA for RalR antitoxin. Toxin RalR functions as a non-specific endonuclease that cleaves methylated and unmethylated DNA. The RNA chaperone Hfq is required for RalA antitoxin activity and appears to stabilize RalA. Also, RalR/RalA is beneficial to the Escherichia coli host for responding to the antibiotic fosfomycin. Hence, our results indicate that cryptic prophage genes can be functionally divergent from their active phage counterparts after integration into the host genome.

Indexed as

Anti-Bacterial AgentsBacterial ToxinsBase PairingDrug Resistance, BacterialEndodeoxyribonucleasesEscherichia coliEscherichia coli ProteinsFosfomycinHost Factor 1 ProteinProtein BiosynthesisRNA, MessengerRNA, Small UntranslatedTranscription FactorsAnti-Bacterial AgentsBacterial ToxinsEndodeoxyribonucleasesEscherichia coli ProteinsFosfomycinHfq protein, E coliHost Factor 1 ProteinRalR protein, E coliRNA, MessengerRNA, Small UntranslatedTranscription Factors

Identifiers

PMID24748661
PMCPMC4041452
OpenAlexW2101923492

What OpenQuestion holds

Textmetadata
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.