Elongation Factors EF Tu and EF G Interact at Related Sites on Ribosomes
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.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- March 1972
- DOI:
- 10.1073/pnas.69.3.752
- Bibcode:
- 1972PNAS...69..752M