Characterization of an Escherichia coli mutant, feeA, displaying resistance to the calmodulin inhibitor 48/80 and reduced expression of the rare tRNALeu3

Nicolas Bouquin, Mao X. Chen, Sunghoon Kim, Françoise Vannier, Sylvie Bernard, I. Barry Holland, Simone J. Séror

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We previously described a mutation feeB1 conferring a temperature-sensitive filamentation phenotype and resistance to the calmodulin inhibitor 48/80 in Escherichia coli, which constitutes a single base change in the acceptor stem of the rare tRNALeu3 recognizing CUA codons. We now describe a second mutant, feeA1, unlinked to feeB, but displaying a similar phenotype, 48/80 resistance and a reduced growth rate at the permissive temperature, 30°C, and temperature-sensitive, forming short filaments at 42°C. In the feeA mutant, tRNALeu3 expression (but not that of tRNALeu1) was reduced approximately fivefold relative to the wild type. We previously showed that the synthesis of β-galactosidase, which unusually requires the translation of 6-CUA codons, was substantially reduced, particularly at 42°C, in feeB mutants. The feeA mutant also shows drastically reduced synthesis of β-galactosidase at the non-permissive temperature and reduced levels even at the permissive temperature. We also show that increased copy numbers of the abundant tRNALeu1, which can also read CUA codons at low efficiency, suppressed the effects of feeA1 under some conditions, providing further evidence that the mutant was deficient in CUA translation. This, and the previous study, demonstrates that mutations which either reduce the activity of tRNALeu3 or the cellular amount of tRNALeu3 confer resistance to the drug 48/80, with concomitant inhibition of cell division at 42°C.

Original languageEnglish
Pages (from-to)853-865
Number of pages13
JournalMolecular Microbiology
Issue number4
Publication statusPublished - 1996 Jan 1


All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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