ArticleMolecular microbiology2022
The UvrA-like protein Ecm16 requires ATPase activity to render resistance against echinomycin.
Article in Molecular microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Self-resistance as a guide to discovering bioactive natural products.Current opinion in chemical biology · 2026Review
- Harnessing Actinobacteria secondary metabolites for tuberculosis drug discovery: Historical trends, current status and future outlooks.Natural products and bioprospecting · 2025Review
- The involvement of multiple ABC transporters in daunorubicin efflux in Streptomyces coeruleorubidus.Microbial biotechnology · 2024Article
- Targeted genome mining for microbial antitumor agents acting through DNA intercalation.Synthetic and systems biotechnology · 2023Article
- Structural and functional analyses of the echinomycin resistance conferring protein Ecm16 from Streptomyces lasalocidi.Scientific reports · 2023Article
- Antibiotic adjuvants: synergistic tool to combat multi-drug resistant pathogens.Frontiers in cellular and infection microbiology · 2023Review
- Proteomic Characterization of Virulence Factors and Related Proteins inInternational journal of molecular sciences · 2022Article
- The UvrA-like protein Ecm16 requires ATPase activity to render resistance against echinomycin.Molecular microbiology · 2022Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Bacteria use various strategies to become antibiotic resistant. The molecular details of these strategies are not fully understood. We can increase our understanding by investigating the same strategies found in antibiotic-producing bacteria. In this work, we characterize the self-resistance protein Ecm16 encoded by echinomycin-producing bacteria. Ecm16 is a structural homolog of the nucleotide excision repair protein UvrA. Expression of ecm16 in the heterologous system Escherichia coli was sufficient to render resistance against echinomycin. Ecm16 binds DNA (double-stranded and single-stranded) using a nucleotide-independent binding mode. Ecm16's binding affinity for DNA increased by 1.7-fold when the DNA is intercalated with echinomycin. Ecm16 can render resistance against echinomycin toxicity independently of the nucleotide excision repair system. Similar to UvrA, Ecm16 has ATPase activity, and this activity is essential for Ecm16's ability to render echinomycin resistance. Notably, UvrA and Ecm16 were unable to complement each other's function. Together, our findings identify new mechanistic details of how a refurbished DNA repair protein Ecm16 can specifically render resistance to the DNA intercalator echinomycin.
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