The role of 2-methylthio-N6-isopentenyladenosine in readthrough and suppression of nonsense codons in Escherichia coli.
Readthrough and suppression of nonsense codons was compared in Escherichia coli strains with and without a miaA mutation, which confers a loss of the isopentenyladenosine modification in transfer RNA. Generally speaking, our results conform to predictions based on previous literature. In addition, we showed that the miaA mutation in strain TRPX is itself a UAA mutation. An antagonism between miaA and rpsL mutations, which confer streptomycin resistance, was also discovered. Our data further suggest that slight alterations of the translation apparatus are easily detectable by monitoring readthrough and suppression of nonsense codons. Our findings are discussed in the context of old and recent reports.
D000241:Adenosine / Q000031:analogs & derivatives*; D003062:Codon; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D007541:Isopentenyladenosine / Q000031:analogs & derivatives* / Q000235:genetics / Q000502:physiology; D009154:Mutation; D014176:Protein Biosynthesis; D000091243:Ribosomal Protein S9; D012269:Ribosomal Proteins / Q000235:genetics; D013489:Suppression, Genetic; D001616:beta-Galactosidase / Q000096:biosynthesis
D003062:Codon; D029968:Escherichia coli Proteins; D000091243:Ribosomal Protein S9; D012269:Ribosomal Proteins; C000717190:RpsI protein, E coli; C008503:2-methylthio-N-6-isopentenyladenosine; D007541:Isopentenyladenosine; D001616:beta-Galactosidase; D000241:Adenosine