Concerning the mode of action of micrococcin upon bacterial protein synthesis.
The antibiotic, micrococcin, binds to complexes formed between bacterial 23-S ribosomal RNA and ribosomal protein L11 and, in doing so, inhibits of thiostrepton. In assay systems simulating partial reaction of protein synthesis, micrococcin inhibits a number of processes believed to involve the ribosomal A site while stimulating GTP hydrolysis dependent upon ribosomes and elongation factor EF-G. The latter effect is not observed upon ribosomes lacking a protein homologous with protein L11. Nor is it apparent upon those containing 23-S RNA previously subjected to the action of a specific methylase known to render ribosomes resistant to thiostrepton. It is concluded that stimulation by micrococcin of factor-dependent GTP hydrolysis results from the binding of the drug to its normal target site which involves 23-S RNA and protein L11.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000096:biosynthesis*; D001430:Bacteriocins; D020558:GTP Phosphohydrolases / Q000378:metabolism; D007700:Kinetics; D010455:Peptides / Q000494:pharmacology; D012269:Ribosomal Proteins / Q000096:biosynthesis*; D012270:Ribosomes / Q000201:enzymology; D013302:Streptomyces / Q000187:drug effects / Q000378:metabolism*; D013883:Thiostrepton / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D001430:Bacteriocins; D010455:Peptides; D012269:Ribosomal Proteins; C027624:ribosomal protein L11; C009779:micrococcin; D020558:GTP Phosphohydrolases; D013883:Thiostrepton