Elongation factor Ts directly facilitates the formation and disassembly of the Escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex. Academic Article uri icon

Overview

MeSH

  • Binding Sites
  • Guanosine Triphosphate
  • Kinetics
  • Models, Molecular
  • Protein Binding
  • Protein Stability
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Spectrometry, Fluorescence

MeSH Major

  • Escherichia coli
  • Escherichia coli Proteins
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors
  • Protein Multimerization
  • RNA, Transfer, Amino Acyl

abstract

  • Aminoacyl-tRNA (aa-tRNA) enters the ribosome in a ternary complex with the G-protein elongation factor Tu (EF-Tu) and GTP. 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). EF-Ts directly facilitates the formation and disassociation of ternary complex. This system demonstrates a novel function of EF-Ts. Aminoacyl-tRNA enters the translating ribosome in a ternary complex with elongation factor Tu (EF-Tu) and GTP. Here, we describe bulk steady state and pre-steady state fluorescence methods that enabled us to quantitatively explore the kinetic features of Escherichia coli ternary complex formation and decay. The data obtained suggest that both processes are controlled by a nucleotide-dependent, rate-determining conformational change in EF-Tu. Unexpectedly, we found that this conformational change is accelerated by elongation factor Ts (EF-Ts), the guanosine nucleotide exchange factor for EF-Tu. Notably, EF-Ts attenuates the affinity of EF-Tu for GTP and destabilizes ternary complex in the presence of non-hydrolyzable GTP analogs. These results suggest that EF-Ts serves an unanticipated role in the cell of actively regulating the abundance and stability of ternary complex in a manner that contributes to rapid and faithful protein synthesis.

publication date

  • May 10, 2013

has subject area

  • Binding Sites
  • Escherichia coli
  • Escherichia coli Proteins
  • Guanosine Triphosphate
  • Kinetics
  • Models, Molecular
  • Peptide Elongation Factor Tu
  • Peptide Elongation Factors
  • Protein Binding
  • Protein Multimerization
  • Protein Stability
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Transfer, Amino Acyl
  • Spectrometry, Fluorescence

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3650427

Digital Object Identifier (DOI)

  • 10.1074/jbc.M113.460014

PubMed ID

  • 23539628

Additional Document Info

start page

  • 13917

end page

  • 13928

volume

  • 288

number

  • 19