Summary
(Yeast) tRNAPhe was modified by reduction in the dihydrouridine loop (tRNA PheRed ) or by acid treatment in the anticodon loop (tRNA Phe-Y ). The non-ribosomal interaction of the tRNAs with codons was determined by binding complementary oligonucleotides. The transfer activities of the tRNAs were studied in a poly(U) dependent system, using ribosomes from a streptomycin-sensitive E. coli strain (L44) and from two streptomycin-resistant mutants (L44-6 and L44-1), which differed in vivo in their degree of restriction.
On wild type ribosomes, streptomycin inhibits phenylalanine transfer by tRNAPhe and does not affect that by tRNA PheRed . Thus, in presence of streptomycin, the transfer activity of tRNAPhe differs from that of tRNA PheRed , whereas in absence of streptomycin tRNA PheRed transfer activity is as good as tRNAPhe transfer activity. The pattern of streptomycin effects was altered in different ways, if ribosomes were used from streptomycin-resistant strains L44-6 and L44-1, respectively. It is suggested that the ribosomal tRNA screen is more complex than consisting of the codon-anticodon binding site only. Streptomycin affects these binding sites in the different ribosomes to a different degree, giving rise to a partial or complete disturbance of the ribosomal tRNA recognition screen.
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Communicated by E. Bautz
Paper No. 90 on “Ribosomal Proteins”. Preceding paper is by Highland et al., J. Mol. Biol., submitted.
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Pongs, O., Nierhaus, K.H. Recognition of normal and modified tRNA by streptomycin sensitive and resistant ribosomes of Escherichia coli . Molec. Gen. Genet. 131, 215–222 (1974). https://doi.org/10.1007/BF00267961
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DOI: https://doi.org/10.1007/BF00267961