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Ribosomal proteins

XXVII. Localization of the amino acid exchanges in protein S5 from two Escherichia coli mutants resistant to spectinomycin

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Summary

Protein S5 which is known to confer sensitivity to the antibiotic spectinomycin has been isolated from 30S subunits of two spectinomycin-resistant mutants. By comparative amino acid analyses of proteins S5 from wild type and mutant as well as by isolation and analyses of the tryptic peptides it was demonstrated that each of the mutants differ from the wild type by replacement of one amino acid only. As shown by amino acid sequence studies the replacements are located within a very short region of protein S5: Peptide T10 of the wild type (val-ser-lys) is changed to glu-ser-lys in one mutant and to val-pro-lys in the other. These findings are discussed together with our previous protein-chemical results on another mutant resistant to spectinomycin.

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References

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Authors and Affiliations

  1. Max-Planck-Institut für Molekulare Genetik, Berlin-Dahlem

    G. Funatsu, E. Schiltz & H. G. Wittmann

Authors
  1. G. Funatsu
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  2. E. Schiltz
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  3. H. G. Wittmann
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Communicated by P. Starlinger

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Funatsu, G., Schiltz, E. & Wittmann, H.G. Ribosomal proteins. Molec. Gen. Genetics 114, 106–111 (1972). https://doi.org/10.1007/BF00332781

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  • DOI: https://doi.org/10.1007/BF00332781

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