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. 1977 Oct;74(10):4341–4345. doi: 10.1073/pnas.74.10.4341

Elongation factor Tu resistant to kirromycin in an Esherichia coli mutant altered in both tuf genes

Eckhard Fischer *,†, Heinz Wolf †, Klaus Hantke †, Andrea Parmeggiani *
PMCID: PMC431937  PMID: 337296

Abstract

A mutant of Escherichia coli is described that displays kirromycin resistance in a cell-free system by virtue of an altered elongation factor Tu (EF-Tu). In poly(U)-directed poly(Phe) synthesis the kirromycin resistance of the crystallized enzyme ranged between a factor of 80 and 700, depending on temperature. Similarly, kirromycin-induced EF-Tu GTPase activity uncoupled from ribosomes and aminoacyl-tRNA required correspondingly higher concentrations of the antibiotic. Resistance of EF-Tu to kirromycin is a consequence of a modified enzyme structure as indicated by its altered fingerprint pattern.

P1 transduction experiments showed that the kirromycin-resistant EF-Tu is coded by an altered tufB gene (tufB1). The known existence of two genes coding for EF-Tu would interfere with the recognition of a mutant altered in only one of those genes, if the mutation were recessive. Because kirromycin blocks EF-Tu release from the ribosome, kirromycin sensitivity is dominant, as shown by the failure of a mixed EF-Tu population to express resistance in vitro. Therefore, phenotypic expression of kirromycin resistance in vivo appears to be only possible if the EF-Tu mutant lacks an active tufA gene, a property likely to be inherited from the parental D22 strain. The observations that introduction of a tufA+ region makes the resistant strain sensitive to the antibiotic and that transduction of tufB1 into a recipient other than E. coli D22 yields kirromycin-sensitive progeny support these conclusions.

Keywords: protein biosynthesis, EF-Tu GTPase regulation, EF-Tu peptide pattern, tufB gene product, dominance of kirromycin sensitivity

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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