Proteinchemical studies on ribosomal proteins S4 and S12 from ram (ribosomal ambiguity) mutants of Escherichia coli
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Proteins S4 and S12 were isolated from ribosomes of three mutants of Escherichia coli in which dependence on streptomycin caused by alteration in protein S12 is suppressed by an altered protein S4. Proteinchemical studies on the mutant proteins gave the following results: Proteins S12 from all three mutants differ from S12 of the wild type by the replacement of proline to leucine in peptide T15. In all mutant S4 proteins a replacement of glutamine to leucine at amino acid position 53 was found. In addition to this replacement at position 53 a glutamic acid residue at position 199 near the C-terminus was deleted in one of the three mutants. However, this deletion is not necessary for the ability of the mutant S4 protein to suppress dependence on streptomycin.
The results support the hypothesis that ram mutants and “revertants” from streptomycin dependence to independence belong to the same class although they were isolated by different selection procedures.
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- Birge, E.A., Kurland, C.G.: Altered ribosomal protein in streptomycin dependent Escherichia coli. Science 166, 1282–1284 (1969)Google Scholar
- Birge, E.A., Kurland, C.G.: Reversion of a streptomycin-dependent strain of Escherichia coli. Molec. gen. Genet. 109, 356–369 (1970)Google Scholar
- Bjare, U., Gorini, L.: Drug dependence reversed by a ribosomal ambiguity mutation, ram, in Escherichia coli. J. molec. Biol. 57, 423–435 (1971)Google Scholar
- Deusser, E., Stöffler, G., Wittmann, H.G., Apirion, D.: Ribosomal proteins. XVI. Altered S4 proteins in Escherichia coli revertants from streptomycin dependence to independence. Molec. gen. Genet. 109, 298–302 (1970)Google Scholar
- Funatsu, G., Schiltz, E., Wittmann, H.G.: Ribosomal proteins. XXVII. Localization of the amino acid exchanges in protein S5 from two Escherichia coli mutants resistant to spectinomycin. Molec. gen. Genet. 114, 106–111 (1971)Google Scholar
- Hasenbank, R., Guthrie, C., Stöffler, G., Wittmann, H.G., Rosen, L., Apirion, D.: Electrophoretic and immunological studies on ribosomal proteins of 100 Escherichia coli revertants from streptomycin dependence. Molec. gen. Genet. 127, 1–18, (1973)Google Scholar
- Hashimoto, K.: Streptomycin resistance in Escherichia coli analysed by transductions. Genetics 45, 49–62 (1960)Google Scholar
- Hindennach, I., Stöffler, G., Wittmann, H.G.: Isolation of the proteins from 30S ribosomal subunits of Escherichia coli. Europ. J. Biochem. 23, 7–11 (1971)Google Scholar
- Kaltschmidt, E., Wittmann, H.G.: Ribosomal proteins. VII. Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Analyt. Biochem. 36, 401–412 (1970)Google Scholar
- Kreider, G., Brownstein, B.L.: A mutation suppressing streptomycin dependence. J. molec. Biol. 61, 135–145 (1971)Google Scholar
- Reinbolt, J., Schiltz, E.: The primary structure of ribosomal protein S4 from Escherichia coli. FEBS Lett. 36, 250–252 (1973)Google Scholar
- Rosset, R., Gorini, L.: A ribosomal ambiguity mutation. J. molec. Biol. 39, 95–112 (1969)Google Scholar
- Wittmann, H. G., Wittmann-Liebold, B.: Chemical structure of bacterial ribosomal proteins. In: “Ribosomes”, Cold Spring Harbor Laboratory Monograph Series, p. 115–140 (1974)Google Scholar
- Wittmann-Liebold, B.: Ribosomal proteins. XXI. Amino acid composition of the tryptic peptides isolated from proteins S4, S18 and S20 of Escherichia coli ribosomes. Hoppe-Seyler's Z. Physiol. Chem. 352, 1705–1714 (1971)Google Scholar
- Zimmermann, R.A., Garvin, R.T., Gorini, L.: Alteration of a 30S ribosomal protein accompanying the ram mutation in Escherichia coli Proc. nat. Acad. Sci. (Wash.) 68, 2263–2267 (1971)Google Scholar