ArticleMolecular microbiology2019
Structural basis of transcriptional regulation by the HigA antitoxin.
Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Ribosomal RNA cleavage by the previously unidentified RelS-RelI toxin-antitoxin system controls growth of Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Characterization of the conjugative modules of the pRAS4 plasmid ofFrontiers in microbiology · 2026Article
- The R plasmid pRAS2 in the fish pathogenFrontiers in microbiology · 2026Article
- Antitoxin control of optimal transcriptional repression in the atypical HigB-HigA toxin-antitoxin system from Proteus vulgaris.Nucleic acids research · 2025Article
- The Putative Virulence Plasmid pYR4 of the Fish PathogenBiology · 2024Article
- Search for Origins of Anti-CRISPR Proteins by Structure Comparison.The CRISPR journal · 2023Article
- Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2023Article
- Article
- A minimal model for gene expression dynamics of bacterial type II toxin-antitoxin systems.Scientific reports · 2021Article
- Article
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
- Structure-based design of peptides that trigger Streptococcus pneumoniae cell death.The FEBS journal · 2021Article
- Article
- Type II Toxin-Antitoxin Systems: Evolution and Revolutions.Journal of bacteriology · 2020Review
- Molecular Characterization of SehB, a Type II Antitoxin ofFrontiers in microbiology · 2020Article
- Structural Insights Into the Transcriptional Regulation of HigBA Toxin-Antitoxin System by Antitoxin HigA inFrontiers in microbiology · 2019Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial toxin-antitoxin systems are important factors implicated in growth inhibition and plasmid maintenance. Type II toxin-antitoxin pairs are regulated at the transcriptional level by the antitoxin itself. Here, we examined how the HigA antitoxin regulates the expression of the Proteus vulgaris higBA toxin-antitoxin operon from the Rts1 plasmid. The HigBA complex adopts a unique architecture suggesting differences in its regulation as compared to classical type II toxin-antitoxin systems. We find that the C-terminus of the HigA antitoxin is required for dimerization and transcriptional repression. Further, the HigA structure reveals that the C terminus is ordered and does not transition between disorder-to-order states upon toxin binding. HigA residue Arg40 recognizes a TpG dinucleotide in higO2, an evolutionary conserved mode of recognition among prokaryotic and eukaryotic transcription factors. Comparison of the HigBA and HigA-higO2 structures reveals the distance between helix-turn-helix motifs of each HigA monomer increases by ~4 Å in order to bind to higO2. Consistent with these data, HigBA binding to each operator is twofold less tight than HigA alone. Together, these data show the HigB toxin does not act as a co-repressor suggesting potential novel regulation in this toxin-antitoxin system.
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