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Molecular and General Genetics MGG

, Volume 142, Issue 1, pp 19–33 | Cite as

Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli

I. Properties of ribosomal mutants whose resistance to neamine is the cumulative effect of two distinct mutations
  • Michel De Wilde
  • Teresa Cabezón
  • Raimundo Villarroel
  • Albert Herzog
  • Alex Bollen
Article

Summary

Two spontaneous mutants of Escherichia coli strain KMBL-146 selected for resistance to the aminoglycoside antibiotic neamine show severe restriction of amber suppressors in vivo. Purified ribosomes from the mutant strains exhibit low neamine-induced misreading in vitro and a decreased affinity for the related antibiotic streptomycin.

Biochemical analysis shows that the mutants each have two modified 30S ribosomal proteins, S12 and S5. In agreement with these results, genetic analysis shows that two mutations are present, neither of which confers resistance to neamine by itself; the mutation located in gene rpxL (the structural gene for protein S12) confers streptomycin dependence but this dependence is suppressed in the presence of the second mutation, located in gene rpxE (the structural gene for protein S5).

Keywords

Escherichia Coli Genetic Analysis Streptomycin Structural Gene Mutant Strain 
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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Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • Michel De Wilde
    • 1
  • Teresa Cabezón
    • 1
  • Raimundo Villarroel
    • 1
  • Albert Herzog
    • 1
  • Alex Bollen
    • 1
  1. 1.Laboratory of GeneticUniversity of BrusselsRhode St GenèseBelgium

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