The Mode of Action of Berninamycin and the Mechanism of Resistance in the Producing Organism, Streptomyces bernensis
- 1 April 1982
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 128 (4) , 875-884
- https://doi.org/10.1099/00221287-128-4-875
Abstract
SUMMARY: The mode of action of berninamycin on bacterial protein synthesis is related to that of thiostrepton, a dissimilar compound. Both antibiotics bind to the complex of 23S RNA with protein L11 and both affect various functions of the ribosomal A site. Also, Streptomyces bernensis and Streptomyces azureus (which, respectively, produce berninamycin and thiostrepton) possess similar ribosomal RNA methylases capable of rendering ribosomes resistant to these compounds. Resistance involves specific pentose-methylation of 23S ribosomal RNA.Keywords
This publication has 10 references indexed in Scilit:
- The Mode of Action of Nosiheptide (Multhiomycin) and the Mechanism of Resistance in the Producing OrganismMicrobiology, 1981
- Concerning the Mode of Action of Micrococcin upon Bacterial Protein SynthesisEuropean Journal of Biochemistry, 1981
- Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11Molecular Genetics and Genomics, 1980
- Resistance to thiostrepton, siomycin, and sporangiomycin in actinomycetes that produce themJournal of Bacteriology, 1980
- Requirement for Ribosomal Protein BM-L1 1 in Stringent Control of RNA Synthesis in Bacillus megateriumEuropean Journal of Biochemistry, 1979
- On the biological role of ribosomal protein BM-L11 of Bacillus megaterium, homologous with Escherichia coli ribosomal protein L11Journal of Molecular Biology, 1979
- Ribosomes in thiostrepton-resistant mutants of Bacillus megaterium lacking a single 50 S subunit proteinJournal of Molecular Biology, 1979
- Binding of Thiostrepton to a Complex of 23‐S rRNA with Ribosomal Protein L11European Journal of Biochemistry, 1979
- Mechanism of resistance to thiostrepton in the producing-organism Streptomyces azureusNature, 1978
- The structures of the highly modified peptide antibiotics micrococcin P1 and P2Journal of the Chemical Society, Chemical Communications, 1978