Evidence for the formation of an unusual ternary complex of rabbit liver EF-1alpha with GDP and deacylated tRNA

FEBS Lett. 1997 Apr 21;407(1):13-7. doi: 10.1016/s0014-5793(97)00242-1.

Abstract

Eukaryotic translation elongation factor 1alpha is known to interact in GTP-bound form with aminoacyl-tRNA promoting its binding to the ribosome. In this paper another ternary complex [EF-1alpha*GDP*deacylated tRNA], never considered in widely accepted elongation schemes, is reported for the first time. The formation of this unusual complex, postulated earlier (FEBS Lett. (1996) 382, 18-20), has been detected by four independent methods. [EF-1alpha*GDP]-interacting sites are located in the acceptor stem, TpsiC stem and TpsiC loop of tRNA(Phe) and tRNA(Leu) molecules. Both tRNA and EF-1alpha are found to undergo certain conformational changes during their interaction. The ability of EF-1alpha to form a complex with deacylated tRNA indicates that the factor may perform an important role in tRNA and aminoacyl-tRNA channeling in higher eukaryotic cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Binding Sites
  • Fluorescence
  • Guanosine Diphosphate / metabolism*
  • Liver / metabolism*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors / metabolism*
  • Protein Biosynthesis
  • RNA, Transfer / metabolism*
  • RNA, Transfer, Leu / metabolism
  • RNA, Transfer, Phe / metabolism
  • Rabbits
  • Ribonucleoproteins / metabolism*
  • Tryptophan / chemistry

Substances

  • Peptide Elongation Factor 1
  • Peptide Elongation Factors
  • RNA, Transfer, Leu
  • RNA, Transfer, Phe
  • Ribonucleoproteins
  • Guanosine Diphosphate
  • Tryptophan
  • RNA, Transfer