ArticleJournal of bacteriology2014
Functional and structural analysis of HicA3-HicB3, a novel toxin-antitoxin system of Yersinia pestis.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Potential role of a CRISPR-Cas-activated toxin-antitoxin system in bacterial immunity.Nature communications · 2026Article
- The Characterization of a Gonococcal HicAB Toxin-Antitoxin System Capable of Causing Bacteriostatic Growth Arrest.Microorganisms · 2025Article
- The HicAB System: Characteristics and Biological Roles of an Underappreciated Toxin-Antitoxin System.International journal of molecular sciences · 2024Review
- Article
- Genomic discovery and structural dissection of a novel type of polymorphic toxin system in gram-positive bacteria.Computational and structural biotechnology journal · 2022Article
- Bacterial toxin-antitoxin modules: classification, functions, and association with persistence.Current research in microbial sciences · 2021Review
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
- The Variety in the Common Theme of Translation Inhibition by Type II Toxin-Antitoxin Systems.Frontiers in genetics · 2020Review
- Article
- Characterization of HicAB toxin-antitoxin module of Sinorhizobium meliloti.BMC microbiology · 2019Article
- Modulation of Toxin-Antitoxin System Rnl AB Type II in Phage-Resistant Gammaproteobacteria Surviving Photodynamic Treatment.Journal of lasers in medical sciences · 2019Review
- The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA.The Journal of biological chemistry · 2018Article
- Functional insights into the Streptococcus pneumoniae HicBA toxin-antitoxin system based on a structural study.Nucleic acids research · 2018Article
- Post-segregational Killing and Phage Inhibition Are Not Mediated by Cell Death Through Toxin/Antitoxin Systems.Frontiers in microbiology · 2018Article
- HicAB toxin-antitoxin complex from Escherichia coli: expression and crystallization.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Desperate times call for desperate measures: benefits and costs of toxin-antitoxin systems.Current genetics · 2017Review
- Article
- The opgC gene is required for OPGs succinylation and is osmoregulated through RcsCDB and EnvZ/OmpR in the phytopathogen Dickeya dadantii.Scientific reports · 2016Article
- Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems.Frontiers in molecular biosciences · 2016Review
- Identification and characterization of the chromosomal yefM-yoeB toxin-antitoxin system of Streptococcus suis.Scientific reports · 2015Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanisms involved in the virulence of Yersinia pestis, the plague pathogen, are not fully understood. In previous research, we found that a Y. pestis mutant lacking the HicB3 (YPO3369) putative orphan antitoxin was attenuated for virulence in a murine model of bubonic plague. Toxin-antitoxin systems (TASs) are widespread in prokaryotes. Most bacterial species possess many TASs of several types. In type II TASs, the toxin protein is bound and neutralized by its cognate antitoxin protein in the cytoplasm. Here we identify the hicA3 gene encoding the toxin neutralized by HicB3 and show that HicA3-HicB3 constitutes a new functional type II TAS in Y. pestis. Using biochemical and mutagenesis-based approaches, we demonstrate that the HicA3 toxin is an RNase with a catalytic histidine residue. HicB3 has two functions: it sequesters and neutralizes HicA3 by blocking its active site, and it represses transcription of the hicA3B3 operon. Gel shift assays and reporter fusion experiments indicate that the HicB3 antitoxin binds to two operators in the hicA3B3 promoter region. We solved the X-ray structures of HicB3 and the HicA3-HicB3 complex; thus, we present the first crystal structure of a TA complex from the HicAB family. HicB3 forms a tetramer that can bind two HicA3 toxin molecules. HicA3 is monomeric and folds as a double-stranded-RNA-binding domain. The HicB3 N-terminal domain occludes the HicA3 active site, whereas its C-terminal domain folds as a ribbon-helix-helix DNA-binding motif.
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