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

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 compl...

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Detalles Bibliográficos
Autores principales: des Georges, Amédée, Hashem, Yaser, Unbehaun, Anett, Grassucci, Robert A., Taylor, Derek, Hellen, Christopher U. T., Pestova, Tatyana V., Frank, Joachim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3950680/
https://www.ncbi.nlm.nih.gov/pubmed/24335085
http://dx.doi.org/10.1093/nar/gkt1279
Descripción
Sumario: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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