ArticleNucleic acids research2017
Toxin inhibition in C. crescentus VapBC1 is mediated by a flexible pseudo-palindromic protein motif and modulated by DNA binding.
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 12 papers.
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12 citing papers in PubMed, 17 citations in OpenAlex.
- Toxin dimerization and a distinct DNA-binding architecture define chromosomal Phd-Doc regulation.Nucleic acids research · 2026Article
- VapC toxins promote the pathogenesis of Rickettsia heilongjiangensis by cleaving essential RNAs from both Rickettsia and its host.PLoS pathogens · 2025Article
- Molecular stripping underpins derepression of a toxin-antitoxin system.Nature structural & molecular biology · 2024Article
- Structural Variations and Rearrangements in Bacterial Type II Toxin-Antitoxin Systems.Sub-cellular biochemistry · 2024Review
- Structural Basis for Toxin Inhibition in the VapXD Toxin-Antitoxin System.Structure (London, England : 1993) · 2021Article
- HEPN RNases - an emerging class of functionally distinct RNA processing and degradation enzymes.Critical reviews in biochemistry and molecular biology · 2021Review
- Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.Nucleic acids research · 2020Article
- VapBC22 toxin-antitoxin system fromScience advances · 2020Article
- Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system.Nature chemical biology · 2019Article
- Structural, functional and biological insights into the role of Mycobacterium tuberculosis VapBC11 toxin-antitoxin system: targeting a tRNase to tackle mycobacterial adaptation.Nucleic acids research · 2018Article
- Structural conservation of the PIN domain active site across all domains of life.Protein science : a publication of the Protein Society · 2017Review
- VapC toxins drive cellular dormancy under uranium stress for the extreme thermoacidophile Metallosphaera prunae.Environmental microbiology · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expression of bacterial type II toxin-antitoxin (TA) systems is regulated at the transcriptional level through direct binding of the antitoxin to pseudo-palindromic sequences on operator DNA. In this context, the toxin functions as a co-repressor by stimulating DNA binding through direct interaction with the antitoxin. Here, we determine crystal structures of the complete 90 kDa heterooctameric VapBC1 complex from Caulobacter crescentus CB15 both in isolation and bound to its cognate DNA operator sequence at 1.6 and 2.7 Å resolution, respectively. DNA binding is associated with a dramatic architectural rearrangement of conserved TA interactions in which C-terminal extended structures of the antitoxin VapB1 swap positions to interlock the complex in the DNA-bound state. We further show that a pseudo-palindromic protein sequence in the antitoxin is responsible for this interaction and required for binding and inactivation of the VapC1 toxin dimer. Sequence analysis of 4127 orthologous VapB sequences reveals that such palindromic protein sequences are widespread and unique to bacterial and archaeal VapB antitoxins suggesting a general principle governing regulation of VapBC TA systems. Finally, a structure of C-terminally truncated VapB1 bound to VapC1 reveals discrete states of the TA interaction that suggest a structural basis for toxin activation in vivo.
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