Concerning the Mode of Action of Micrococcin upon Bacterial Protein Synthesis

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Abstract
The antibiotic, micrococcin, binds to complexes formed between bacterial (Escherichia coli) 23 S rRNA and ribosomal protein L11 and, in doing so, inhibits the binding of thiostrepton. In assay systems simulating partial reactions of proteins synthesis, micrococcin inhibits a number of processes believed to involve the ribosomal A site while stimulating GTP hydrolysis dependent on ribosomes and elongation factor EF-G. The latter effect is not observed on ribosomes lacking a protein homologous with protein L11, and is also not apparent on ribosomes containing 23 S RNA subjected to the action of a specific methylase known to render ribosomes resistant to thiostrepton. 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.