Functional interactions between mutated forms of ribosomal proteins S4, S5 and S12.
Here we show that ram mutations, either in ribosomal protein S4 or S5, decrease the proofreading flows for both cognate and noncognate ternary complexes bound by streptomycin-dependent (SmD) ribosomes. This effect is accompanied by a slight increase in the overall error frequency. More important, however, is the decreased proofreading of the cognate species which is almost reduced to wild-type levels. The data suggest that it may be the reduction of the proofreading of the cognate substrate that is important for suppressing streptomycin dependence. Furthermore, we show that rpsE mutants, selected from streptomycin-dependent strains, behave kinetically very similarly to the previously described rpsD mutants.
D003062:Codon; D004926:Escherichia coli / Q000235:genetics*; D007700:Kinetics; D009154:Mutation; D010641:Phenotype; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013307:Streptomycin / Q000494:pharmacology; D001616:beta-Galactosidase / Q000235:genetics
D003062:Codon; D012333:RNA, Messenger; D012269:Ribosomal Proteins; D001616:beta-Galactosidase; D013307:Streptomycin