title: 30S subunit mutations relieving restriction of ribosomal misreading caused by L6 mutations.
abstract: Mutants were analyzed biochemically and genetically in which restriction of translational misreading by ribosomes containing an altered L6 protein is relieved. Amongst 100 such strains eight possessed an altered S4 and two a mutant S5 protein. The protein-chemical type of L6 mutation seems to influence the kind of S4 mutant form selected. Also, only a few types of S4 ram mutations are obtained and they are different from those usually found amongst suppressors of streptomycin-dependent (SmD) strains. The S4 mutations selected are able to reduce the level of streptomycin-resistance of strA1 or strA40 strains and they confer extreme hypersensitivity to aminoglycosides when present alone. On the other hand, S4 mutations from SmD suppressor strains only weakly reverse L6 restriction. The results imply that control of translational fidelity is an intersubunit function and that protein L6 (an interface protein) cooperates with 30S proteins by directly or indirectly determining parameters involved in aminoacyl-tRNA recognition.
mesh_terms: D000617:Aminoglycosides / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D009154:Mutation; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000235:genetics; D012269:Ribosomal Proteins / Q000235:genetics*; D014161:Transduction, Genetic
chemical_list: D000617:Aminoglycosides; D012269:Ribosomal Proteins; D012343:RNA, Transfer