ArticleThe Journal of biological chemistry2009
Bacterial toxin HigB associates with ribosomes and mediates translation-dependent mRNA cleavage at A-rich sites.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed.
- Article
- Identification of a novel gene inAntimicrobial agents and chemotherapy · 2026Article
- The HigB-like SehA toxin promotes non-replicating Salmonella inside macrophages by inhibiting ribonuclease III-dependent rRNA maturation.Nucleic acids research · 2026Article
- Carrot and stick: how RNase R contributes to function and destruction of the translation machinery.RNA biology · 2025Review
- N-acetyl-glucosamine primes Pseudomonas aeruginosa for virulence through a type IV pili/cAMP-mediated morphology transition.Nature communications · 2025Article
- Antitoxin control of optimal transcriptional repression in the atypical HigB-HigA toxin-antitoxin system from Proteus vulgaris.Nucleic acids research · 2025Article
- Article
- A single vector system for tunable and homogeneous dual gene expression in Escherichia coli.Scientific reports · 2025Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- Toxin-antitoxin systems in bacterial pathogenesis.Heliyon · 2023Review
- The endogenous Coxiella burnetii plasmid encodes a functional toxin-antitoxin system.Molecular microbiology · 2022Article
- Toxin-antitoxin systems in pathogenic3 Biotech · 2022Review
- Substrate recognition and cryo-EM structure of the ribosome-bound TAC toxin of Mycobacterium tuberculosis.Nature communications · 2022Article
- Functional characterization of HigBA toxin-antitoxin system in an Arctic bacterium, Bosea sp. PAMC 26642.Journal of microbiology (Seoul, Korea) · 2022Article
- Genome diversity of domesticatedMicrobial genomics · 2022Article
- Insights into the Neutralization and DNA Binding of Toxin-Antitoxin System ParEMicroorganisms · 2021Article
- Bacterial toxin-antitoxin modules: classification, functions, and association with persistence.Current research in microbial sciences · 2021Review
- A minimal model for gene expression dynamics of bacterial type II toxin-antitoxin systems.Scientific reports · 2021Article
- ThemSphere · 2021Article
- Genome Mining Shows Ubiquitous Presence and Extensive Diversity of Toxin-Antitoxin Systems inFrontiers in microbiology · 2021Article
25 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
Abstract
Most pathogenic Proteus species are primarily associated with urinary tract infections, especially in persons with indwelling catheters or functional/anatomic abnormalities of the urinary tract. Urinary tract infections caused by Proteus vulgaris typically form biofilms and are resistant to commonly used antibiotics. The Rts1 conjugative plasmid from a clinical isolate of P. vulgaris carries over 300 predicted open reading frames, including antibiotic resistance genes. The maintenance of the Rts1 plasmid is ensured in part by the HigBA toxin-antitoxin system. We determined the precise mechanism of action of the HigB toxin in vivo, which is distinct from other known toxins. We demonstrate that HigB is an endoribonuclease whose enzymatic activity is dependent on association with ribosomes through the 50 S subunit. Using primer extension analysis of several test mRNAs, we showed that HigB cleaved extensively across the entire length of coding regions only at specific recognition sequences. HigB mediated cleavage of 100% of both in-frame and out-of-frame AAA sequences. In addition, HigB cleaved approximately 20% of AA sequences in coding regions and occasionally cut single As. Remarkably, the cleavage specificity of HigB coincided with one of the most frequently used codons in the AT-rich Proteus spp., AAA (lysine). Therefore, the HigB-mediated plasmid maintenance system for the Rts1 plasmid highlights the intimate relationship between host cells and extrachromosomal DNA that enables the dynamic acquisition of genes that impart a spectrum of survival advantages, including those encoding multidrug resistance and virulence factors.
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