Structure of the mammalian ribosomal pre-termination complex associated with eRF1.eRF3.GDPNP

Nucleic Acids Res. 2014 Mar;42(5):3409-18. doi: 10.1093/nar/gkt1279. Epub 2013 Dec 11.

Abstract

Eukaryotic translation termination results from the complex functional interplay between two release factors, eRF1 and eRF3, in which GTP hydrolysis by eRF3 couples codon recognition with peptidyl-tRNA hydrolysis by eRF1. Here, we present a cryo-electron microscopy structure of pre-termination complexes associated with eRF1•eRF3•GDPNP at 9.7 -Å resolution, which corresponds to the initial pre-GTP hydrolysis stage of factor attachment and stop codon recognition. It reveals the ribosomal positions of eRFs and provides insights into the mechanisms of stop codon recognition and triggering of eRF3's GTPase activity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Codon, Terminator
  • GTP Phosphohydrolases / metabolism
  • Guanosine Triphosphate / analogs & derivatives
  • Guanosine Triphosphate / chemistry
  • Humans
  • Models, Molecular
  • Peptide Chain Termination, Translational*
  • Peptide Termination Factors / chemistry*
  • Peptide Termination Factors / metabolism
  • Ribosomes / chemistry*

Substances

  • Codon, Terminator
  • ETF1 protein, human
  • GDPNP compound
  • Peptide Termination Factors
  • peptide-chain-release factor 3
  • Guanosine Triphosphate
  • GTP Phosphohydrolases

Associated data

  • PDB/3J5Y