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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Dec;64(4):1388–1395. doi: 10.1073/pnas.64.4.1388

THE ROLE OF RIBOSOMAL CONFORMATION IN PROTEIN BIOSYNTHESIS: THE STREPTOMYCIN-RIBOSOME INTERACTION*

Michael I Sherman 1,2, Melvin V Simpson 1,2
PMCID: PMC223297  PMID: 4916926

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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