Open AccessTHE ROLE OF RIBOSOMAL CONFORMATION IN PROTEIN BIOSYNTHESIS: THE STREPTOMYCIN-RIBOSOME INTERACTION
Author(s) -
Michael I. Sherman,
Melvin V. Simpson
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.64.4.1388
Subject(s) - ribosome , streptomycin , ribosomal rna , protein biosynthesis , genetic code , ribosomal protein , translation (biology) , biology , chemistry , biochemistry , messenger rna , rna , amino acid , gene , antibiotics
The role played by ribosomal conformation in codon-anticodon recognition has been studied using streptomycin as a probe, inasmuch as streptomycin is known to cause misreading of the genetic code. Changes in ribosomal structure have been followed by the method of hydrogen-tritium exchange. The results show that streptomycin induces two types of change in the hydrogen exchange pattern. At low molar ratios of streptomycin to ribosomes, a stimulation of the hydrogen exchange rate (“loosening” of ribosomal structure) is observed, with a small inhibition of polypeptide synthesis. As the streptomycin: ribosome ratio is increased, a maximum exchange rate is reached, after which the rate decreases (“tightening” of structure); in this region, inhibition of peptide synthesis increases sharply, and misreading of the code begins. None of these effects is observed with streptomycin-resistant ribosomes.