Summary
The capability of ribosomes of four types of streptomycin-resistant mutants (A1, A2, A40 and A60) for non-enzymatic (EF-G-GTP-independent) translocation was tested. It was found that an A40 type mutation (amino acid replacement in position 87 of the protein S12 polypeptide chain) leads to activation of the capability of the ribosome to perform spontaneous non-enzymatic translocation, while type A1, A2 and A60 mutations (amino acid replacements in position 42 of protein S12) does not give such an effect. Thus, it is shown that non-enzymatic translocation can be activated not only by the earlier described damage of the protein S12 by para-chloromercuribenzoate or by the complete removal of protein S12, but also by a definite mutational alteration of the protein. Preliminary data are also reported on the possibility of activating non-enzymatic translocation by combinations of mutational alterations of the ribosomal proteins other than protein S12 but interdepending with it (such as S4 and S5).
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References
Birge, E., Kurland, C. G.: Reversion of a streptomycin dependent strain of Escherichia coli. Molec. gen. Genet. 109, 356–369 (1970)
Bollen, A., Davies, J., Ozaki, M., Mizushima, S.: Ribosomal protein conferring sensitivity to the antibiotic spectinomycin in Escherichia coli. Science 165, 85–86 (1969)
Breckenridge, L., Gorini, L.: Genetic analysis of streptomycin resistance in Escherichia coli. Genetics 65, 9–25 (1970)
Dekio, S., Takata, R.: Genetic studies of the ribosomal proteins in Escherichia coli. II. Altered 30 S ribosomal protein component specific to spectinomycin resistant mutants. Molec. gen. Genet. 105, 219–224 (1969)
Deusser, E., Stöffler, G., Wittmann, H. G., Apirion, D.: Ribosomal proteins. XVI. Altered S 4 proteins in Escherichia coli revertants from streptomycin dependence to independence. Molec. gen. Genet. 109, 298–302 (1970)
Erbe, R. W., Nau, M. M., Leder, P.: Translation and translocation of defined RNA messengers. J. molec. Biol. 39, 441–460 (1969).
Funatsu, G., Nierhaus, K., Wittmann, H. G.: Ribosomal proteins. XXXVII. Determination of allelle types and amino acid exchanges in protein S12 of three streptomycin-resistant mutants of Escherichia coli. Biochim. biophys. Acta (Amst.) 287, 282–291 (1972a)
Funatsu, G., Nierhaus, K., Wittmann-Liebold, B.: Ribosomal proteins. XXII. Studies on the altered protein S5 from a spectinomycin resistant mutant of Escherichia coli. J. molec. Biol. 64, 201–209 (1972b)
Funatsu, G., Wittmann, H. G.: Ribosomal proteins. XXXIII. Location of amino acid replacements in protein S12 isolated from Escherichia coli mutants resistant to streptomycin. J. molec. Biol. 68, 547–550 (1972)
Gavrilova, L. P., Koteliansky, V. E.: “Non-enzymatic” translation of oligouridylates of different length. Dokl. Akad. Nauk SSSR 220, 1211–1213 (1975)
Gavrilova, L. P., Spirin, A. S.: Stimulation of “non-enzymic” translocation in ribosomes by p-chloromercuribenzoate. FEBS Letters 17, 324–326 (1971)
Gavrilova, L. P., Spirin, A. S.: A modification of the 30 S ribosomal subparticle is responsible for stimulation of “non-enzymatic” translocation by p-chloromercuribenzoate. FEBS Letters 22, 91–92 (1972)
Gavrilova, L. P., Spirin, A. S.: Interaction of SH-reagents with the ribosomal 30 S subparticle and “non-enzymatic” translocation. FEBS Letters 39, 13–16 (1974)
Gavrilova, L. P., Koteliansky, V. E., Spirin, A. S.: Ribosomal protein S12 and “non-enzymatic” translocation. FEBS Letters 45, 324–328 (1974)
Hasenbank, R., Guthrie, C., Stöffler, G., Wittmann, H. G., Rosen, L., Apirion, D.: Electrophoretic and immunology studies on ribosomal proteins of 100 Escherichia coli revertants from streptomycin dependence. Molec. gen. Genet. 127, 1–18 (1973)
Kreider, G., Brownstein, B. L.: A mutation suppressing streptomycin dependence. II. An altered protein in the 30 S ribosomal proteins. J. molec. Biol. 61, 135–142 (1971)
Kreider, G., Brownstein, B. L.: Ribosomal proteins involved in the suppression of streptomycin dependence in Escherichia coli. J. Bact. 109, 780–785 (1972)
Ozaki, M., Mizushima, S., Nomura, M.: Identification and functional characterization of the protein controlled by the streptomycin-resistant locus in E. coli. Nature (Lond.) 222, 333–339 (1969)
Pestka, S.: Studies on the formation of transfer ribonucleic acid-ribosome complexes. III. The formation of peptide bonds by ribosomes in the absence of supernatant enzymes. J. biol. Chem. 243, 2810–2820 (1968)
Stöffler, G., Deusser, E., Wittmann H. G., Apirion, D.: Ribosomal proteins. XIX. Altered S5 ribosomal protein in an Escherichia coli revertant from streptomycin dependence to independence. Molec. gen. Genet. 111, 334–341 (1971)
Tissières, A., Watson, J. D., Schlessinger, D., Hollingworth, B. R.: Ribonucleoprotein particles from E. coli. J. molec. Biol. 1, 221–233 (1959)
Zimmermann, R. A., Carvin, R. T., Gorini, L.: Alteration of a 30 S ribosomal protein accompanying the ram mutation in Escherichia coli Proc. nat. Acad. Sci. (Wash.) 68, 2263–2267 (1971)
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Asatryan, L.S., Spirin, A.S. Non-enzymatic translocation in ribosomes from streptomycin-resistant mutants of Escherichia coli . Molec. Gen. Genet. 138, 315–321 (1975). https://doi.org/10.1007/BF00264801
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DOI: https://doi.org/10.1007/BF00264801