Studies on the role of factor Ts in polypeptide synthesis

Elongation Factor Ts Directly Facilitates the Formation and Disassembly of the Escherichia coli Elongation Factor Tu·GTP·Aminoacyl-tRNA Ternary Complex

“…1D). In striking contrast to contemporary models in which EF-Ts serves only as the GEF for EF-Tu (49,62), these findings collectively led us to examine whether EF-Ts functions to regulate ternary complex stability in a direct manner through modulation of the nucleotide binding site.…”

Moonlighting Functions of Polypeptide Elongation Factor 1: From Actin Bundling to Zinc Finger Protein R1-Associated Nuclear Localization

“…3) One of the most important accomplishments in the E. coli translation system was the resolution of EF-T into EF-Tu and EF-Ts, the former of which catalyzes the binding of aa-tRNA to the ribosome, 4) and the latter catalyzes the exchange of GDP W GTP on EF-Tu・GDP. 5) EF-2 has been puriˆed from various organisms and shown to be a nearly 100-kDa monomeric protein having translocase and ribosome-dependent GTPase activities. 6,7) EF-1 puriˆed from rabbit reticulocytes was reported to be a trimer of identical 62-kDa subunits that e‹ciently catalyzed aa-tRNA binding to ribosomes, 8) and EF-1 was shown to have nearly equal dissociation constants for GDP and GTP.…”

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

“…During the elongation stage, GTP participates with elongation factor EF Tu in the binding of aminoacyl-tRNA to the ribosome as part of the intermediate aminoacyl-tRNA*EF Tu GTP complex (2,3). When this complex interacts with the ribosome, GTP is hydrolyzed, aminoacyl-tRNA is bound to the ribosome, and EF Tu GDP is released (4,5). After peptide bond formation, hydrolysis of GTP, catalyzed by factor EF G, is required for ejection of the deacylated tRNA (6) and for the translocation of the ribosome along the message (7,8).…”