Abstract
The Escherichia coli suppressor mutation, supT, has been shown to cause a C --> U substitution in the middle position of the tRNA(GGG) (Gly) anticodon. This is the same tRNA species that is altered by the glyUsu(AGA) mutation studied previously. This finding indicates that the supT mutant tRNA reads the glutamic acid codon, GAG. The supT suppressor has also been converted to a new suppressor, called glyUsu(GAA), which will suppress the GAA mutation, trpA46. The in vivo suppression efficiencies of each of these three missense suppressors has been measured and are as follows: glyUsu(AGA), 3.6%; supT, 1.6%; and glyUsu(GAA), 0.4%. Mistranslation by these mutant glycine tRNA species has no adverse affects on cell growth since cultures possessing the suppressors grow as fast as cells without. The supT tRNA species can be observed as a peak in the profile of glycyl-tRNA fractionated on a RPC-5 chromatographic column, indicating that the mutant tRNA can be aminoacylated with reasonable efficiency. This finding contrasts with previous findings concerning the glyUsu(AGA) mutant tRNA which is not significantly aminoacylated under the same conditions.
MeSH Terms
Carbon Radioisotopes
Chromatography
Escherichia coli/growth & development,metabolism
Genetic Code
Glycine
Mutation
Oligonucleotides/analysis
Phosphorus Radioisotopes
Polyribonucleotide Nucleotidyltransferase
Protein Biosynthesis
RNA, Bacterial/analysis,metabolism
RNA, Transfer/analysis,metabolism
Recombination, Genetic
Ribonucleases
Suppression, Genetic
Transduction, Genetic
Chemicals
Carbon Radioisotopes
Oligonucleotides
Phosphorus Radioisotopes
RNA, Bacterial
RNA, Transfer
Polyribonucleotide Nucleotidyltransferase
Ribonucleases
Glycine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hill C W
Combriato G
Dolph W
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22 references, click to expand
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