Ribosomal protein alterations in thiostrepton- and Micrococcin-resistant mutants of Bacillus subtilis.
Ribosomal proteins of parental thiostrepton- and micrococcin-sensitive Bacillus subtilis cysA14 and thiostrepton-and micrococcin-resistant mutants were compared. Several electrophoretic and immunochemical techniques showed unambiguously that BS-L11 was not present on 50 S ribosomal subunits from the six thiostrepton-resistant mutants. Protein BS-L11 reappeared in all six revertants from thiostrepton resistance to thiostrepton sensitivity. No definitive protein alteration could be ascribed to the mutation from micrococcin sensitivity to resistance. It was also demonstrated that B. subtilis protein BS-L11 is homologous to Escherichia coli ribosomal protein L11. The finding that ribosomes from thiostrepton-resistant mutants do not contain protein L11 suggests that L11 not only is involved in binding of thiostrepton, but also, when mutationally altered, confers resistance to this antibiotic. Although the ribosomes of these strains do not contain protein L11, all thiostrepton-resistant mutants showed the same viability as the parental strain. Thus protein L11 cannot be obligatory for the structure and function of the ribosome.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000187:drug effects / Q000378:metabolism*; D004352:Drug Resistance, Microbial; D004588:Electrophoresis, Cellulose Acetate; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D009154:Mutation; D010455:Peptides / Q000494:pharmacology; D012269:Ribosomal Proteins / Q000378:metabolism*; D013045:Species Specificity; D013883:Thiostrepton / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D010455:Peptides; D012269:Ribosomal Proteins; D013883:Thiostrepton