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Nucleic Acids Research, 1991, Vol. 19, No. 4 867-869
© 1991

MOLECULAR BIOLOGY

Suppression of a double missense mutation by a mutant Phe tRNAPhe in Escherichia coli

Dominique Pages, Kathy Hijazi1, Emanuel Murgola1, Jacqueline Finelli and Richard H. Buckingham*

Institut de Biologie Physico-Chimique 13 rue Pierre et Marie Curie, 75005 Paris, France 1Department of Molecular Genetics, The University of Texas M.D.Anderson Cancer Center 1515 Holcombe Boulevard, Houston, TX 77030, USA

* To whom correspondence should be addressed

Received October 17, 1990. Revised December 12, 1990. Accepted December 12, 1990.

We report here the isolation of a mutant tRNAPhe that suppresses a double missense auxotrophic mutation in trpA of Escherichia coil, trpA218. The doubly mutant protein product dtffers from wild-type TrpA by the replacements of Phe22 by Leu and Gly211 by Ser. A partial revertant TrpA phenotype can be obtained from trpA218 by changing either Leu22 back to Phe or Ser211 back to Gly. Translational suppressors werepreviously obtained that act at codon 211, replacing the Ser211 in the TrpA218 protein, presumably with Gly. In the present study, we selected for trpA218 suppressors caused by mutatlon of a cloned tRNAPhe gene, pheV. DNA sequence analysis of the suppressor Isolated reveals a singular structural aiteration, changing the anticodon from 5'GAA-3' to 5'-GAG-3'. Sequencing of trpA218 confirmed the likely identity of Leu22 as CUC. The new missense suppressor, designated pheV(SuCUC), is iethal to the cell when highly expressed, as from a high copy number plasmid. This may be due to efficient replacement of Leu by Phe at CUC (and, probably, CUU) codons throughout the genome. We anticipate that pheV(SuCUC) will prove, like other missense suppressors, to be extremely useful in studies on the specificity and accuracy of decoding.


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