ArticleNucleic acids research2017
Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 57 citations in OpenAlex.
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- Antitoxin control of optimal transcriptional repression in the atypical HigB-HigA toxin-antitoxin system from Proteus vulgaris.Nucleic acids research · 2025Article
- ChiraKit: an online tool for the analysis of circular dichroism spectroscopy data.Nucleic acids research · 2025Article
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- Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025Article
- Mechanisms of neutralization of toxSAS from toxin-antitoxin modules.Nature chemical biology · 2025Article
- A single vector system for tunable and homogeneous dual gene expression in Escherichia coli.Scientific reports · 2025Article
- Ubiquitin-derived artificial binding proteins targeting oncofetal fibronectin reveal scaffold plasticity by β-strand slippage.Communications biology · 2024Article
- Fuzzy recognition by the prokaryotic transcription factor HigA2 from Vibrio cholerae.Nature communications · 2024Article
- Structural Variations and Rearrangements in Bacterial Type II Toxin-Antitoxin Systems.Sub-cellular biochemistry · 2024Review
- Conformational features and interaction mechanisms of VProtein science : a publication of the Protein Society · 2023Article
- The structural basis of hyperpromiscuity in a core combinatorial network of type II toxin-antitoxin and related phage defense systems.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
- The endogenous Coxiella burnetii plasmid encodes a functional toxin-antitoxin system.Molecular microbiology · 2022Article
- Molecular basis of anti-CRISPR operon repression by Aca10.Nucleic acids research · 2022Article
- Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila.Nature communications · 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
- Genome diversity of domesticatedMicrobial genomics · 2022Article
- Structural basis for anti-CRISPR repression mediated by bacterial operon proteins Aca1 and Aca2.The Journal of biological chemistry · 2021Article
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxin-antitoxin (TA) modules are small operons involved in bacterial stress response and persistence. higBA operons form a family of TA modules with an inverted gene organization and a toxin belonging to the RelE/ParE superfamily. Here, we present the crystal structures of chromosomally encoded Vibrio cholerae antitoxin (VcHigA2), toxin (VcHigB2) and their complex, which show significant differences in structure and mechanisms of function compared to the higBA module from plasmid Rts1, the defining member of the family. The VcHigB2 is more closely related to Escherichia coli RelE both in terms of overall structure and the organization of its active site. VcHigB2 is neutralized by VcHigA2, a modular protein with an N-terminal intrinsically disordered toxin-neutralizing segment followed by a C-terminal helix-turn-helix dimerization and DNA binding domain. VcHigA2 binds VcHigB2 with picomolar affinity, which is mainly a consequence of entropically favorable de-solvation of a large hydrophobic binding interface and enthalpically favorable folding of the N-terminal domain into an α-helix followed by a β-strand. This interaction displaces helix α3 of VcHigB2 and at the same time induces a one-residue shift in the register of β-strand β3, thereby flipping the catalytically important Arg64 out of the active site.
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