Elongation factors EF Tu and EF G interact at related sites on ribosomes.
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.
D004926:Escherichia coli / Q000032:analysis; D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational; D010759:Phosphorus Isotopes; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000032:analysis / Q000378:metabolism*
D010759:Phosphorus Isotopes; D006160:Guanosine Triphosphate; D012343:RNA, Transfer