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

Benjamin J. Burnett, Roger B. Altman, Ryan Ferrao, Jose L. Alejo, Navdep Kaur, Joshua Kanji, Scott C. Blanchard

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)13917-13928
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number19
DOIs
StatePublished - May 10 2013

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