Summary
Telve chloramphenicol resistant (CM r)-mutants were isolated from B. subtilis ATCC 6633 and were classified into the following six groups.
Group I. No 50s ribosomal protein change was detectable. Ribosomes did not show alteration of the binding ability to CM or to erythromycin in vitro.
Group II. A 50s protein, 50a, was altered. Ribosomes did not show alteration of the binding ability to CM or to erythromycin in vitro. The genes specifying the 50a protein was in the cysA-str region on B. subtilis chromosome.
Group III. A 50s protein, 50b, was altered. Biological properties of the ribosomes were the same as Group I or II so fas as examined. The genes for 50b protein was in the cysA-str region.
Group IV. A 50s protein, 50c, was altered. Ribosomes showed a definite decrease in ability to bind to CM in vitro. The binding of erythromycin to the ribosomes was not impaired. The chromosomal locus of the CM r (and for 50c protein) was in the cysA-str region.
Group V. A 50s protein, 50e, was changed. The ability of the ribosomes to bind in vitro both to CM and to erythromycin was greatly reduced. The genetic locus of the CM r (and for 50e protein) was in the cysA-str region.
Group VI. A 50s protein, 50f, was altered. Ribosomes showed a decrease in ability to bind in vitro both to CM and to erythromycin. The genes for 50f protein was in the cysA-str region.
The results suggest that the ribosomal resistance to CM may be caused by an independent change of at least several 50s ribosomal protein species. The genetic data shown here and those reported previously show that at least two 30s and seven 50s ribosomal protein genes are situated in the cysA-str region on B. subtilis chromosome.
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References
Fernandez-Muñoz, R., Monro, R. E., Torres-Pinedo, R., Vazquez, D.: Substrate- and antibiotic-binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol, lincomycin and erythromycin sites. Europ. J. Biochem. 23, 185–193 (1971)
Kimura, A., Kobata, K., Takata, R., Osawa, S.: Genetic and chemical studies on the ribosomes from spectinomycin resistant mutants of Bacillus subtilis. Molec. gen. Genet. 124, 107–115 (1973)
Nirenberg, M. W.: In: Methods in enzymology (S. P. Colowick and N. O. Kaplan, eds.), vol. 6, p. 17. New York: Academic Press 1963
Oelinick, N. L., Wilhelm, J. M., Corcoran, J. W.: Nonidentity of the site of action of erythromycin A and chloramphenicol on Bacillus subtilis ribosomes. Biochim. biophys. Acta (Amst.) 155, 290–292 (1968)
Osawa, S., Otaka, E., Takata, R., Dekio, S., Matsubara, M., Itoh, T., Muto, A., Tanaka, K., Teroka, H., Tamaki, M.: Ribosomal protein genes in bacteria. FEBS Symposium, vol. 23, p. 313–336. London: Academic Press 1972
Otaka, E., Teraoka, H., Tamaki, M., Tanaka, K., Osawa, S.: Ribosomes from erythromycin-resistant mutants of Escherichia coli Q13. J. molec. Biol. 48, 499–510 (1970)
Smith, I., Goldthwaite, C., Dubnau, D.: The genetics of ribosomes in Bacillus subtilis. Cold Spr. Harb. Symp. quant. Biol. 34, 85–89 (1969)
Takata, R.: Genetic studies of the ribosomal proteins in Escherichia coli. VIII. Mapping of ribosomal protein components by intergeneric mating experiments between Serratia marcescens and Escherichia coli. Molec. gen. Genet. 118, 363–371 (1972)
Tanaka, K., Tamaki, M., Kimura, A., Takata, R., Osawa, S.: Low affinity for chloramphenicol of erythromycin resistant Escherichia coli ribosomes having an altered protein component. Biochem. biophys. Res. Commun. 46, 1979–1983 (1972)
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Communicated by H. G. Wittmann
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Osawa, S., Takata, R., Tanaka, K. et al. Chloramphenicol resistant mutants of Bacillus subtilis . Molec. Gen. Genet. 127, 163–173 (1973). https://doi.org/10.1007/BF00333664
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DOI: https://doi.org/10.1007/BF00333664