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Alteration of ribosomal protein S5 from two spectinomycin-resistant mutants of Bacillus subtilis: Deletion of one amino acid residue

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Summary

The ribosomal protein S5 was isolated from Bacillus subtilis ATCC 6633 (wild-type) and two spectinomycin-resistant mutants (BSPC 31 and BSPC 61). Analyses of the protein revealed that in each of these mutants one of the two consecutive arginine residues (position 29 or 30 in the wild-type) is missing.

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References

  • Higo K, Otaka E, Osawa S (1982) Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: Correlation to Escherichia coli 30S proteins. Mol Gen Genet (in press)

  • Itoh T (1976) Amino acid replacement in the protein S5 from a spectinomycin resistant mutant of Bacillus subtilis. Mol Gen Genet 144:39–42

    Google Scholar 

  • Itoh T, Kosugi H, Higo K, Osawa S (1975) Ribosomal proteins from streptomycin-resistant and dependent mutants, and revertants from streptomycin-dependence to independence in Bacillus subtilis. Mol Gen Genet 139:293–301

    Google Scholar 

  • Kimura A, Kobata K, Takata R, Osawa S (1973) Genetic and chemical studies of ribosomes from spectinomycin resistant mutants of Bacillus subtilis. Mol Gen Genet 124:107–115

    Google Scholar 

  • Wittman HG, Littlechild JA, Wittmann-Liebold B (1980) Structure of ribosomal proteins. In: Chambliss G, Craven GR, Davies J, Davis K, Kahan L, Nomura M (eds) Ribosomes: structure, function, and genetics. University Park Press, Baltimore, Maryland, p 51

    Google Scholar 

  • Wittmann-Liebold B, Greuer B (1978) The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome. FEBS Lett 95:91–98

    Google Scholar 

  • Yaguchi M, Visentin LP, Nazar RN, Matheson AT (1978) Structure and thermal stability of ribosomal components from thermophilic bacteria. In: Friedman SM (ed) Biochemistry of thermophily. Academic Press, New York, p 169

    Google Scholar 

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Author notes

  1. Syozo Osawa

    Present address: Laboratory of Molecular Genetics, Department of Biology, Nagoya University, 464, Nagoya, Japan

Authors and Affiliations

  1. Department of Biochemistry and Biophysics, Research Institute for Nuclear Medicine and Biology, Hiroshima University, Kasumi, Minami-ku, 734, Hiroshima, Japan

    Ken-ichi Higo, Takuzi Itoh & Syozo Osawa

Authors
  1. Ken-ichi Higo
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  2. Takuzi Itoh
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  3. Syozo Osawa
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Communicated by K. Isono

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Higo, Ki., Itoh, T. & Osawa, S. Alteration of ribosomal protein S5 from two spectinomycin-resistant mutants of Bacillus subtilis: Deletion of one amino acid residue. Molec. Gen. Genet. 185, 205–206 (1982). https://doi.org/10.1007/BF00330787

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  • DOI: https://doi.org/10.1007/BF00330787

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