Initiation of translation at AUC, AUA and AUU codons in Escherichia coli.
A truncated form of the HBL murein hydrolase, encoded by the temperate bacteriophage HB-3, was cloned in a pUC-derivative and translated in Escherichia coli using AUC as start codon, as confirmed by biochemical, immunological, and N-terminal analyses. Using site-directed mutagenesis, we have changed this AUC codon into AUA, AUU and AUG codons. The relative translation efficiencies for these triplets were about 5% for AUC and AUU and 7.5% for AUA compared to that of AUG codon. In the same gene arrangement E. coli beta-galactosidase was also translated at moderate efficiency using AUC as initiator.
Unidad de Genética Bacteriana, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
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A
Romero
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García
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000235:genetics; D001483:Base Sequence; D003062:Codon / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics*; D010442:Peptide Chain Initiation, Translational / Q000235:genetics*; D013296:Streptococcus pneumoniae / Q000235:genetics; D001616:beta-Galactosidase / Q000235:genetics
D003062:Codon; D001616:beta-Galactosidase; D009238:N-Acetylmuramoyl-L-alanine Amidase