ArticleThe Journal of biological chemistry2014
Structural and functional characterization of Escherichia coli toxin-antitoxin complex DinJ-YafQ.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Characterization of the conjugative modules of the pRAS4 plasmid ofFrontiers in microbiology · 2026Article
- A plasmid-encoded inactive toxin-antitoxin system MtvT/MtvA regulates plasmid conjugative transfer and bacterial virulence in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- Functional characterization and transcriptional repression by Lacticaseibacillus paracasei DinJ-YafQ.Applied microbiology and biotechnology · 2022Article
- Insights into the Neutralization and DNA Binding of Toxin-Antitoxin System ParEMicroorganisms · 2021Article
- Strategies to Investigate Membrane Damage, Nucleoid Condensation, and RNase Activity of Bacterial Toxin-Antitoxin Systems.Methods and protocols · 2021Article
- Characterization of DinJ-YafQ toxin-antitoxin module in Tetragenococcus halophilus: activity, interplay, and evolution.Applied microbiology and biotechnology · 2021Article
- Rapid growth inhibitory activity of a YafQ-family endonuclease toxin of the Helicobacter pylori tfs4 integrative and conjugative element.Scientific reports · 2020Article
- Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.Nucleic acids research · 2020Article
- Identification and first characterization of DinJ-YafQ toxin-antitoxin systems in Lactobacillus species of biotechnological interest.Scientific reports · 2019Article
- New Shuttle Vectors for Gene Cloning and Expression in Multidrug-Resistant Acinetobacter Species.Antimicrobial agents and chemotherapy · 2018Article
- Production, biophysical characterization and crystallization of Pseudomonas putida GraA and its complexes with GraT and the graTA operator.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism.Nucleic acids research · 2017Article
- Mechanism of endonuclease cleavage by the HigB toxin.Nucleic acids research · 2016Article
- Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems.Frontiers in molecular biosciences · 2016Review
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- Molecular basis of ribosome recognition and mRNA hydrolysis by the E. coli YafQ toxin.Nucleic acids research · 2015Article
- Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxin YafQ functions as a ribonuclease in the dinJ-yafQ toxin-antitoxin system of Escherichia coli. Antitoxin DinJ neutralizes YafQ-mediated toxicity by forming a stable protein complex. Here, crystal structures of the (DinJ)2-(YafQ)2 complex and the isolated YafQ toxin have been determined. The structure of the heterotetrameric complex (DinJ)2-(YafQ)2 revealed that the N-terminal region of DinJ folds into a ribbon-helix-helix motif and dimerizes for DNA recognition, and the C-terminal portion of each DinJ exclusively wraps around a YafQ molecule. Upon incorporation into the heterotetrameric complex, a conformational change of YafQ in close proximity to the catalytic site of the typical microbial ribonuclease fold was observed and validated. Mutagenesis experiments revealed that a DinJ mutant restored YafQ RNase activity in a tetramer complex in vitro but not in vivo. An electrophoretic mobility shift assay showed that one of the palindromic sequences present in the upstream intergenic region of DinJ served as a binding sequences for both the DinJ-YafQ complex and the antitoxin DinJ alone. Based on structure-guided and site-directed mutagenesis of DinJ-YafQ, we showed that two pairs of amino acids in DinJ were important for DNA binding; the R8A and K16A substitutions and the S31A and R35A substitutions in DinJ abolished the DNA binding ability of the DinJ-YafQ complex.
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Registered trials
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