Direct evidence of an elongation factor-Tu/Ts·GTP·Aminoacyl-tRNA quaternary complex. Academic Article uri icon

Overview

MeSH

  • Escherichia coli
  • Models, Molecular
  • Ribosomes

MeSH Major

  • Escherichia coli Proteins
  • Guanosine Triphosphate
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors
  • RNA, Transfer, Amino Acyl

abstract

  • During protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribosomes. In so doing, EF-Tu increases the rate and fidelity of the translation mechanism. Recent evidence suggests that EF-Ts, the guanosine nucleotide exchange factor for EF-Tu, directly accelerates both the formation and dissociation of the EF-Tu-GTP-Phe-tRNA(Phe) ternary complex (Burnett, B. J., Altman, R. B., Ferrao, R., Alejo, J. L., Kaur, N., Kanji, J., and Blanchard, S. C. (2013) J. Biol. Chem. 288, 13917-13928). A central feature of this model is the existence of a quaternary complex of EF-Tu/Ts·GTP·aa-tRNA(aa). Here, through comparative investigations of phenylalanyl, methionyl, and arginyl ternary complexes, and the development of a strategy to monitor their formation and decay using fluorescence resonance energy transfer, we reveal the generality of this newly described EF-Ts function and the first direct evidence of the transient quaternary complex species. These findings suggest that EF-Ts may regulate ternary complex abundance in the cell through mechanisms that are distinct from its guanosine nucleotide exchange factor functions. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

publication date

  • August 22, 2014

has subject area

  • Escherichia coli
  • Escherichia coli Proteins
  • Guanosine Triphosphate
  • Models, Molecular
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors
  • RNA, Transfer, Amino Acyl
  • Ribosomes

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4156062

Digital Object Identifier (DOI)

  • 10.1074/jbc.M114.583385

PubMed ID

  • 24990941

Additional Document Info

start page

  • 23917

end page

  • 23927

volume

  • 289

number

  • 34