ArticleThe Journal of biological chemistry2018
The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Potential role of a CRISPR-Cas-activated toxin-antitoxin system in bacterial immunity.Nature communications · 2026Article
- Hidden diversity inMicrobiology spectrum · 2025Article
- Gentamicin induction of the gonococcalmBio · 2025Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- The HicAB System: Characteristics and Biological Roles of an Underappreciated Toxin-Antitoxin System.International journal of molecular sciences · 2024Review
- Article
- Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2023Article
- Complete Genome Sequence of SMBL-WEM22, a Halotolerant Strain of Kosakonia cowanii Isolated from Hong Kong Seawater.Microbiology resource announcements · 2021Article
- Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.Acta crystallographica. Section D, Structural biology · 2021Article
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
- Comparative Genomic Analyses and CRISPR-Cas Characterization ofFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Toxin-antitoxin (TA) systems are present in many bacteria and play important roles in bacterial growth, physiology, and pathogenicity. Those that are best studied are the type II TA systems, in which both toxins and antitoxins are proteins. The HicAB system is one of the prototypic TA systems, found in many bacterial species. Complex interactions between the protein toxin (HicA), the protein antitoxin (HicB), and the DNA upstream of the encoding genes regulate the activity of this system, but few structural details are available about how HicA destabilizes the HicB-DNA complex. Here, we determined the X-ray structures of HicB and the HicAB complex to 1.8 and 2.5 Å resolution, respectively, and characterized their DNA interactions. This revealed that HicB forms a tetramer and HicA and HicB form a heterooctameric complex that involves structural reorganization of the C-terminal (DNA-binding) region of HicB. Our observations indicated that HicA has a profound impact on binding of HicB to DNA sequences upstream of
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Registered trials
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