Effects of miaA on translation and growth rates.
We have measured the growth rates and elongation rates for different proteins in wild-type, miaA, rpsL, and miaA, rpsL double mutants of Escherichia coli in the presence as well as the absence of streptomycin. The data show that while miaA and rpsL mutants inhibit elongation rates to equivalent levels, miaA inhibits the growth rate twice as effectively as does rpsL. The double mutant is more effectively inhibited than either single mutant and Sm repairs in part the growth rate as well as protein elongation rates. The data suggest that the conditional streptomycin-dependent phenotype of the double mutant cannot be due simply to the depressed polypeptide elongation rates of the double mutant.
Diaz
I
I
Department of Molecular Biology, Biomedical Center, Uppsala, Sweden.
Pedersen
S
S
Kurland
C G
CG
D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development*; D029968:Escherichia coli Proteins; D007700:Kinetics; D009154:Mutation; D010441:Peptide Chain Elongation, Translational; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000235:genetics; D000091243:Ribosomal Protein S9; D013997:Time Factors; D014158:Transcription, Genetic
D029968:Escherichia coli Proteins; D000091243:Ribosomal Protein S9; C000717190:RpsI protein, E coli; D012343:RNA, Transfer