ArticleBioscience reports2015
Identification of Escherichia coli ygaQ and rpmG as novel mitomycin C resistance factors implicated in DNA repair.
Article in Bioscience reports, 2015. 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.
- Transcriptomic Responses of MRSA to Penicillin-Modulating Phlorotannins Derived fromMarine drugs · 2026Article
- From Design to Practice: A Comprehensive Tutorial for the Rapid Multiplex Engineering ofBio-protocol · 2026Article
- Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655.BMC microbiology · 2026Article
- Identification of antimicrobial resistance genes in Escherichia coli through network diffusion.The Journal of antimicrobial chemotherapy · 2026Article
- Efflux pump inhibitor chlorpromazine effectively increases the susceptibility ofFuture microbiology · 2024Article
- Novel Genes Required for Surface-Associated Motility in Acinetobacter baumannii.Current microbiology · 2021Article
- Protein structure, amino acid composition and sequence determine proteome vulnerability to oxidation-induced damage.The EMBO journal · 2020Article
- Efficiency of induction of Shiga-toxin lambdoid prophages in Escherichia coli due to oxidative and antibiotic stress depends on the combination of prophage and the bacterial strain.Journal of applied genetics · 2020Article
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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
Using the ASKA (A Complete Set of Escherichia coli K-12 ORF Archive) library for genome-wide screening of E. coli proteins we identified that expression of ygaQ and rpmG promotes mitomycin C resistance (MMC(R)). YgaQ mediated MMC(R) was independent of homologous recombination involving RecA or RuvABC, but required UvrD. YgaQ is an uncharacterized protein homologous with α-amylases that we identified to have nuclease activity directed to ssDNA of 5' flaps. Nuclease activity was inactivated by mutation of two amino acid motifs, which also abolished MMC(R). RpmG is frequently annotated as a bacterial ribosomal protein, although forms an operon with MutM glycosylase and a putative deubiquitinating (DUB) enzyme, YicR. RpmG associated MMC(R) was dependent on MutM. MMC(R) from RpmG resembles DNA repair phenotypes reported for 'idiosyncratic ribosomal proteins' in eukaryotes.
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