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

Research output: Contribution to journalArticle

49 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)6448-6462
Number of pages15
JournalNucleic acids research
Volume42
Issue number10
DOIs
StatePublished - 2014

Fingerprint

Antitoxins
Deoxyribonucleases
RNA
Escherichia coli
Prophages
Fosfomycin
Endonucleases
DNA
Bacteriophages
Genes
scorpion toxin I''
Nucleotides
Genome
Anti-Bacterial Agents
Messenger RNA

All Science Journal Classification (ASJC) codes

  • Genetics

Cite this

Guo, Yunxue ; Quiroga, Cecilia ; Chen, Qin ; McAnulty, Michael J. ; Benedik, Michael J. ; Wood, Thomas K. ; Wang, Xiaoxue. / RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system in Escherichia coli. In: Nucleic acids research. 2014 ; Vol. 42, No. 10. pp. 6448-6462.
@article{1399c2229c5c4e50a0c7fe9311dc63cd,
title = "RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system in Escherichia coli",
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.",
author = "Yunxue Guo and Cecilia Quiroga and Qin Chen and McAnulty, {Michael J.} and Benedik, {Michael J.} and Wood, {Thomas K.} and Xiaoxue Wang",
year = "2014",
doi = "10.1093/nar/gku279",
language = "English (US)",
volume = "42",
pages = "6448--6462",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "10",

}

Guo, Y, Quiroga, C, Chen, Q, McAnulty, MJ, Benedik, MJ, Wood, TK & Wang, X 2014, 'RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system in Escherichia coli', Nucleic acids research, vol. 42, no. 10, pp. 6448-6462. https://doi.org/10.1093/nar/gku279

RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system in Escherichia coli. / Guo, Yunxue; Quiroga, Cecilia; Chen, Qin; McAnulty, Michael J.; Benedik, Michael J.; Wood, Thomas K.; Wang, Xiaoxue.

In: Nucleic acids research, Vol. 42, No. 10, 2014, p. 6448-6462.

Research output: Contribution to journalArticle

TY - JOUR

T1 - RalR (a DNase) and RalA (a small RNA) form a type I toxin-antitoxin system in Escherichia coli

AU - Guo, Yunxue

AU - Quiroga, Cecilia

AU - Chen, Qin

AU - McAnulty, Michael J.

AU - Benedik, Michael J.

AU - Wood, Thomas K.

AU - Wang, Xiaoxue

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84903215390&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84903215390&partnerID=8YFLogxK

U2 - 10.1093/nar/gku279

DO - 10.1093/nar/gku279

M3 - Article

C2 - 24748661

AN - SCOPUS:84903215390

VL - 42

SP - 6448

EP - 6462

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 10

ER -