ArticleNature communications2017
GyrI-like proteins catalyze cyclopropanoid hydrolysis to confer cellular protection.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Emerging antibiotic resistance by various novel proteins/enzymes.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Review
- Functional and Structure Prediction of Hypothetical Proteins FromBioMed research international · 2025Article
- Intracellularly driven chemical modifications of antimicrobial secondary metabolites: Potent mechanisms of self-resistance.Pharmaceutical science advances · 2024Review
- YgiV promoter mutations cause resistance to cystobactamids and reduced virulence factor expression in Escherichia coli.npj antimicrobials and resistance · 2024Article
- Newly Discovered Mechanisms of Antibiotic Self-Resistance with Multiple Enzymes Acting at Different Locations and Stages.Antibiotics (Basel, Switzerland) · 2022Review
- Biosynthesis of DNA-Alkylating Antitumor Natural Products.Molecules (Basel, Switzerland) · 2022Review
- A Specialized Polythioamide-Binding Protein Confers Antibiotic Self-Resistance in Anaerobic Bacteria.Angewandte Chemie (International ed. in English) · 2022Article
- TEX264 at the intersection of autophagy and DNA repair.Autophagy · 2022Review
- Reductive inactivation of the hemiaminal pharmacophore for resistance against tetrahydroisoquinoline antibiotics.Nature communications · 2021Article
- Structural evolution of a DNA repair self-resistance mechanism targeting genotoxic secondary metabolites.Nature communications · 2021Article
- Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway.Trends in biochemical sciences · 2019Review
Corrections and comments
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GyrI-like proteins are widely distributed in prokaryotes and eukaryotes, and recognized as small-molecule binding proteins. Here, we identify a subfamily of these proteins as cyclopropanoid cyclopropyl hydrolases (CCHs) that can catalyze the hydrolysis of the potent DNA-alkylating agents yatakemycin (YTM) and CC-1065. Co-crystallography and molecular dynamics simulation analyses reveal that these CCHs share a conserved aromatic cage for the hydrolytic activity. Subsequent cytotoxic assays confirm that CCHs are able to protect cells against YTM. Therefore, our findings suggest that the evolutionarily conserved GyrI-like proteins confer cellular protection against diverse xenobiotics via not only binding, but also catalysis.
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Registered trials
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