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Molecular and General Genetics MGG

, Volume 142, Issue 1, pp 35–43 | Cite as

Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli

II. Localization of amino acid replacements in proteins S5 and S12 altered in double mutants resistant to neamine
  • M. Yaguchi
  • H. G. Wittmann
  • T. Cábezon
  • M. De Wilde
  • R. Villarroel
  • A. Herzog
  • A. Bollen
Article

Summary

Protein S5 and S12 were isolated from 30S ribosomal subunits of two E. coli mutants highly resistant to the antibiotic neamine, and of the parental strain. Proteinchemical analyses on these proteins led to the following results: a) In protein S5 the arginine residue in peptide T2 of the parental strain is replaced by glycine in one (nea 314) or serine in the other (nea 319) of the two mutants. b) In protein S12 the proline residue in peptide T15 of the parental strain is replaced by leucine in mutant nea 314 and by glutamine in mutant nea 319.

Comparison of these results with those obtained in earlier studies on other mutants with altered ribosomal proteins revealed that the amino acid replacements in neamine resistant mutants and in “revertants” from streptomycin dependence occur at the same amino acid positions of proteins S5 and S12. Therefore it is likely that both types of mutants belong to the same class.

Keywords

Peptide Glycine Serine Proline Arginine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • M. Yaguchi
    • 1
  • H. G. Wittmann
    • 1
  • T. Cábezon
    • 2
  • M. De Wilde
    • 2
  • R. Villarroel
    • 2
  • A. Herzog
    • 2
  • A. Bollen
    • 2
  1. 1.Max-Planck-Institut für Molekulare GenetikBerlin-DahlemGermany
  2. 2.Laboratory of GeneticsUniversity of BrusselsRhode St. GeneseBelgium

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