ArticleNucleic acids research2012
Crystal structure of the DNA-bound VapBC2 antitoxin/toxin pair from Rickettsia felis.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 55 citations in OpenAlex.
- Editorial for Special Issue "Molecular Research in Vaccinology and Vaccine Development".Current issues in molecular biology · 2026Article
- Article
- Toxin:antitoxin ratio sensing autoregulation of theScience advances · 2024Article
- Structural Variations and Rearrangements in Bacterial Type II Toxin-Antitoxin Systems.Sub-cellular biochemistry · 2024Review
- Impact of Genomic Deletion RD16 on the Expression of theCurrent issues in molecular biology · 2023Article
- Metagenome diversity illuminates origins of pathogen effectors.bioRxiv : the preprint server for biology · 2023Article
- Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.Nucleic acids research · 2020Article
- Review
- Crystal Structure of VapBC-1 from Nontypeable Haemophilus influenzae and the Effect of PIN Domain Mutations on Survival during Infection.Journal of bacteriology · 2019Article
- Toxins targeting transfer RNAs: Translation inhibition by bacterial toxin-antitoxin systems.Wiley interdisciplinary reviews. RNA · 2019Review
- The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA.The Journal of biological chemistry · 2018Article
- Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Nucleic acids research · 2017Article
- 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
- Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.Journal of molecular biology · 2017Article
- Toxin inhibition in C. crescentus VapBC1 is mediated by a flexible pseudo-palindromic protein motif and modulated by DNA binding.Nucleic acids research · 2017Article
- Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.Journal of bacteriology · 2016Article
- Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic Bacteria.Toxins · 2016Review
- Article
- Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems.Frontiers in molecular biosciences · 2016Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Besides their commonly attributed role in the maintenance of low-copy number plasmids, toxin/antitoxin (TA) loci, also called 'addiction modules', have been found in chromosomes and associated to a number of biological functions such as: reduction of protein synthesis, gene regulation and retardation of cell growth under nutritional stress. The recent discovery of TA loci in obligatory intracellular species of the Rickettsia genus has prompted new research to establish whether they work as stress response elements or as addiction systems that might be toxic for the host cell. VapBC2 is a TA locus from R. felis, a pathogen responsible for flea-borne spotted fever in humans. The VapC2 toxin is a PIN-domain protein, whereas the antitoxin, VapB2, belongs to the family of swapped-hairpin β-barrel DNA-binding proteins. We have used a combination of biophysical and structural methods to characterize this new toxin/antitoxin pair. Our results show how VapB2 can block the VapC2 toxin. They provide a first structural description of the interaction between a swapped-hairpin β-barrel protein and DNA. Finally, these results suggest how the VapC2/VapB2 molar ratio can control the self-regulation of the TA locus transcription.
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