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

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1972 Mar 1

PMID 4551986

Citations 17

Authors

D L Miller

Affiliations

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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.

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