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PMID: 765735 Published · ppublish English Journal Article

Cooperative control of translation fidelity by ribosomal proteins in Escherichia coli. I. Properties of ribosomal mutants whose resistance to neamine is the cumulative effect of two distinct mutations.

Molecular & general genetics : MGG ·Vol. 142 ·No. 1 ·1975-12-23 ·Pages 19-33

De Wilde M, Cabezón T, Villarroel R, Herzog A, Bollen A

Abstract

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 ribosmal 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).

MeSH Terms
Chromosome Mapping Chromosomes, Bacterial Drug Resistance, Microbial Escherichia coli/drug effects,metabolism Genes Mutation Neomycin/pharmacology Protein Biosynthesis Ribosomal Proteins/metabolism Streptomycin/pharmacology
Chemicals
Ribosomal Proteins Neomycin Streptomycin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
De Wilde M
Cabezón T
Villarroel R
Herzog A
Bollen A
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27 references, click to expand
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Article Info
Journal
Molecular & general genetics : MGG
Abbr.
Mol Gen Genet
ISSN
0026-8925
Published
1975-12-23
Pages
19-33
Language
English
Region
Germany
NLM ID
0125036
Subset
IM
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