Molecular and General Genetics MGG

, Volume 140, Issue 1, pp 61–68

Proteinchemical studies on ribosomal proteins S4 and S12 from ram (ribosomal ambiguity) mutants of Escherichia coli

Authors

  • Ute van Acken
    • Abt. WittmannMax-Planck-Institut für Molekulare Genetik
    • Dr. U. van AckenRobert-Koch-Institut
Article

DOI: 10.1007/BF00268989

Cite this article as:
van Acken, U. Molec. Gen. Genet. (1975) 140: 61. doi:10.1007/BF00268989

Summary

Proteins S4 and S12 were isolated from ribosomes of three mutants of Escherichia coli in which dependence on streptomycin caused by alteration in protein S12 is suppressed by an altered protein S4. Proteinchemical studies on the mutant proteins gave the following results: Proteins S12 from all three mutants differ from S12 of the wild type by the replacement of proline to leucine in peptide T15. In all mutant S4 proteins a replacement of glutamine to leucine at amino acid position 53 was found. In addition to this replacement at position 53 a glutamic acid residue at position 199 near the C-terminus was deleted in one of the three mutants. However, this deletion is not necessary for the ability of the mutant S4 protein to suppress dependence on streptomycin.

The results support the hypothesis that ram mutants and “revertants” from streptomycin dependence to independence belong to the same class although they were isolated by different selection procedures.

Copyright information

© Springer-Verlag 1975