Mutant ribosomes can generate dominant kirromycin resistance.

doi:10.1128/jb.173.12.3635-3643.1991

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Article

Mutant ribosomes can generate dominant kirromycin resistance.

Journal of bacteriology - 1 Jun 1991

Tubulekas I, Buckingham R H, Hughes D

Abstract excerpt

Mutations in the two genes for EF-Tu in Salmonella typhimurium and Escherichia coli, tufA and tufB, can confer resistance to the antibiotic kirromycin. Kirromycin resistance is a recessive phenotype expressed when both tuf genes are mutant. We describe a new kirromycin-resistant phenotype dominant to the effect of wild-type EF-Tu. Strains carrying a single kirromycin-resistant tuf mutation and an...

Topics

Base Sequence
DNA, Bacterial
Drug Resistance, Microbial
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Kinetics
Molecular Sequence Data
Peptide Elongation Factor Tu
Phenotype
Polymerase Chain Reaction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Biosynthesis

Pyridones

Ribosomal Protein S9

Ribosomes

Salmonella typhimurium

Species Specificity

Streptomycin

Source

Open in PubMed Open full text

Identifiers

PMID: 2050625
DOI: 10.1128/jb.173.12.3635-3643.1991
PMCID: PMC207990

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2050625-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mutant ribosomes can generate dominant kirromycin resistance.PMID 2050625Read ↗

Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli.Semantic proximity Read ↗

The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli.Semantic proximity Read ↗

Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP.Semantic proximity Read ↗

A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome.Semantic proximity Read ↗

Antisuppression by mutations in elongation factor Tu.Semantic proximity Read ↗

Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors.Semantic proximity Read ↗

Mutants of EF-Tu defective in binding aminoacyl-tRNA.Semantic proximity Read ↗

Reducing ppGpp level rescues an extreme growth defect caused by mutant EF-Tu.Semantic proximity Read ↗

Phenotypic Suppression of Streptomycin Resistance by Mutations in Multiple Components of the Translation Apparatus.Semantic proximity Read ↗

Knockout of tusA confers cationic antimicrobial resistance via fur and omp genes in Escherichia coli.Semantic proximity Read ↗

Impaired in vitro kinetics of EF-Tu mutant Aa.Semantic proximity Read ↗

GE2270A-resistant mutations in elongation factor Tu allow productive aminoacyl-tRNA binding to EF-Tu.GTP.GE2270A complexes.Semantic proximity Read ↗

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