Abstract
THE antibiotic, thiostrepton, produced by Streptomyces azureus, inhibits bacterial protein synthesis by binding to 50S ribosomal subunits with 1:1 stoichiometry. Recently1, we showed that S. azureus prevents its own death by methylating 23S ribosomal RNA (rRNA) so that its ribosomes do not bind the drug. Intact ribosomes are not substrates for the methylase and those experiments involved methylation of ‘core particles’ derived from the (thiostrepton-sensitive) ribosomes of Streptomyces coelicolor. Ribosomes can be reconstituted from core particles by adding back the missing ‘split proteins’. Presumably, in S. azureus, methylation of 23S rRNA occurs before assembly of the 50S ribosomal subunit is completed. Here we report that the ‘thiostrepton-resistance’ methylase of S. azureus is an RNA-ribose methylase which introduces a single methyl group into adenosine in 23S rRNA. This is a novel antibiotic-resistance mechanism.
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CUNDLIFFE, E., THOMPSON, J. Ribose methylation and resistance to thiostrepton. Nature 278, 859–861 (1979). https://doi.org/10.1038/278859a0
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DOI: https://doi.org/10.1038/278859a0
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