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. 1972 Mar;69(3):752–755. doi: 10.1073/pnas.69.3.752

Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes

David Lee Miller 1
PMCID: PMC426550  PMID: 4551986

Abstract

The binding of elongation factor EF G to ribosomes inhibits the subsequent reaction of the ribosomes with the ternary complex aminoacyl-tRNA·EF Tu·GTP. Both the hydrolysis of GTP and the binding of aminoacyl-tRNA to ribosomes are nearly abolished by the previous binding of factor EF G to ribosomes in the presence of either fusidic acid plus either GTP or a nonhydrolyzable analog of GTP. The results suggest that each elongation factor binds to the same region on the ribosome. The GTPase activities of both factors EF G and EF Tu may be activated by interaction at the same ribosomal site, as has been previously suggested by others.

Keywords: aminoacyl-tRNA binding, GTP hydrolysis, fusidic acid, chloramphenicol, GMPPCP

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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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