Antisuppression by a mutation in rpsM(S13) giving a shortened ribosomal protein S13.

摘要: The phenotype associated with an rpsM(S13) mutation, originally isolated in Escherichia coli a selection for pseudoreversion of streptomycin dependence, was studied strains lacking the original mutations antibiotic dependence. rpsM mutation gives decreased translational step time and reduced growth rate. It functions as strong antisuppressor to both serU(Su1) amber suppressor trpT(Su9) opal suppressor, whereas tyrT(Su3) is much less affected. small ribosomal subunit from mutant shows sedimentation coefficient but able form apparently normal 70S ribosomes judged by ultracentrifugational analysis. Cloning sequencing show that CAG TAG alteration at codon position 100, giving S13 protein which shortened 19 amino acids its C-terminal end. This implies domain involved binding 16S RNA should be