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. 1971 Apr;68(4):805–809. doi: 10.1073/pnas.68.4.805

Conformational Changes in Ribosomes during Protein Synthesis

Max H Schreier 1,*, Hans Noll 1,†
PMCID: PMC389048  PMID: 4927674

Abstract

In a purified system containing poly(U) and ribosomal subunits from Escherichia coli, and purified transfer factors T and G, the active ribosomal complex passes through a cycle of contraction and expansion with the addition of each amino acid; aminoacyl-tRNA binding catalyzed by T produces the stable compact state, corresponding to the 70S conformation, whereas translocation with G expands the ribosome to a less stable 60S form. It is also shown that formation of the first peptide bond must be preceded by translocation with G. These findings are consistent with a model of chain initiation in the absence of initiation factors in which deacylated tRNAPhe bound to the P site signals translocation by G and GTP as soon as the 60S initiation complex has been converted to the 70S form by the enzymatic binding of Phe-tRNA.

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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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