ArticleAntimicrobial agents and chemotherapy2009
A novel insertion mutation in Streptomyces coelicolor ribosomal S12 protein results in paromomycin resistance and antibiotic overproduction.
Article in Antimicrobial agents and chemotherapy, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 31 citations in OpenAlex.
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- Development of a Fluorescence Polarization Assay for Multi-Determination of 10 Aminoglycosides in Pork Muscle Sample Based on Ribosomal Protein S12 and Studying Its Recognition Mechanism.Foods (Basel, Switzerland) · 2022Article
- A novel mechanism of streptomycin resistance in Yersinia pestis: Mutation in the rpsL gene.PLoS neglected tropical diseases · 2021Article
- The Application of Regulatory Cascades inFrontiers in microbiology · 2020Review
- Combined Drug Resistance Mutations Substantially Enhance Enzyme Production in Paenibacillus agaridevorans.Journal of bacteriology · 2018Article
- Substantial improvement of toyocamycin production in Streptomyces diastatochromogenes by cumulative drug-resistance mutations.PloS one · 2018Article
- Identification of a Novel Lincomycin Resistance Mutation Associated with Activation of Antibiotic Production in Streptomyces coelicolor A3(2).Antimicrobial agents and chemotherapy · 2017Article
- Insights into microbial cryptic gene activation and strain improvement: principle, application and technical aspects.The Journal of antibiotics · 2017Review
- Screening and analysis on the protein interaction of the protein VP7 in grass carp reovirus.Virus genes · 2015Article
- Streptomycin resistance-aided genome shuffling to improve doramectin productivity of Streptomyces avermitilis NEAU1069.Journal of industrial microbiology & biotechnology · 2013Article
- Disruption of rimP-SC, encoding a ribosome assembly cofactor, markedly enhances the production of several antibiotics in Streptomyces coelicolor.Microbial cell factories · 2013Article
- New strategies for drug discovery: activation of silent or weakly expressed microbial gene clusters.Applied microbiology and biotechnology · 2013Review
- Cinnamic acid production using Streptomyces lividans expressing phenylalanine ammonia lyase.Journal of industrial microbiology & biotechnology · 2011Article
- Novel two-component systems implied in antibiotic production in Streptomyces coelicolor.PloS one · 2011Article
- Antibiotic overproduction by rpsL and rsmG mutants of various actinomycetes.Applied and environmental microbiology · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We identified a novel paromomycin resistance-associated mutation in rpsL, caused by the insertion of a glycine residue at position 92, in Streptomyces coelicolor ribosomal protein S12. This insertion mutation (GI92) resulted in a 20-fold increase in the paromomycin resistance level. In combination with another S12 mutation, K88E, the GI92 mutation markedly enhanced the production of the blue-colored polyketide antibiotic actinorhodin and the red-colored antibiotic undecylprodigiosin. The gene replacement experiments demonstrated that the K88E-GI92 double mutation in the rpsL gene was responsible for the marked enhancement of antibiotic production observed. Ribosomes with the K88E-GI92 double mutation were characterized by error restrictiveness (i.e., hyperaccuracy). Using a cell-free translation system, we found that mutant ribosomes harboring the K88E-GI92 double mutation but not ribosomes harboring the GI92 mutation alone displayed sixfold greater translation activity relative to that of the wild-type ribosomes at late growth phase. This resulted in the overproduction of actinorhodin, caused by the transcriptional activation of the pathway-specific regulatory gene actII-orf4, possibly due to the increased translation of transcripts encoding activators of actII-orf4. The mutant with the K88E-GI92 double mutation accumulated a high level of ribosome recycling factor at late stationary phase, underlying the high level of protein synthesis activity observed.
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