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

Amédée Des Georges; Yaser Hashem; Anett Unbehaun; Robert A. Grassucci; Derek Taylor; Christopher U.T. Hellen; Tatyana V. Pestova; Joachim Frank

doi:10.1093/nar/gkt1279

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

Amédée Des Georges, Yaser Hashem, Anett Unbehaun, Robert A. Grassucci, Derek Taylor, Christopher U.T. Hellen, Tatyana V. Pestova, Joachim Frank

Molecular Pathobiology

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	3409-3418
Number of pages	10
Journal	Nucleic acids research
Volume	42
Issue number	5
DOIs	https://doi.org/10.1093/nar/gkt1279
State	Published - Mar 1 2014

ASJC Scopus subject areas

Genetics

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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 -{\AA} 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.",

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AU - Des Georges, Amédée

AU - Hashem, Yaser

AU - Unbehaun, Anett

AU - Grassucci, Robert A.

AU - Taylor, Derek

AU - Hellen, Christopher U.T.

AU - Pestova, Tatyana V.

AU - Frank, Joachim

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AB - 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.

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

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