Elongation factor Ts directly facilitates the formation and disassembly of the escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex

Abstract

Background: Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP. Results: EF-Tu·GTP·aa-tRNA ternary complex formation and decay rates are accelerated in the presence of the nucleotide exchange factor elongation factor Ts (EF-Ts). Conclusion: EF-Ts directly facilitates the formation and disassociation of ternary complex. Significance: This system demonstrates a novel function of EF-Ts. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.