Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1

Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to...

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Autores principales: Preis, Anne, Heuer, Andre, Barrio-Garcia, Clara, Hauser, Andreas, Eyler, Daniel E., Berninghausen, Otto, Green, Rachel, Becker, Thomas, Beckmann, Roland
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6813808/
https://www.ncbi.nlm.nih.gov/pubmed/25001285
http://dx.doi.org/10.1016/j.celrep.2014.04.058
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author Preis, Anne
Heuer, Andre
Barrio-Garcia, Clara
Hauser, Andreas
Eyler, Daniel E.
Berninghausen, Otto
Green, Rachel
Becker, Thomas
Beckmann, Roland
author_facet Preis, Anne
Heuer, Andre
Barrio-Garcia, Clara
Hauser, Andreas
Eyler, Daniel E.
Berninghausen, Otto
Green, Rachel
Becker, Thomas
Beckmann, Roland
author_sort Preis, Anne
collection PubMed
description Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complex containing eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination.
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spelling pubmed-68138082019-10-25 Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1 Preis, Anne Heuer, Andre Barrio-Garcia, Clara Hauser, Andreas Eyler, Daniel E. Berninghausen, Otto Green, Rachel Becker, Thomas Beckmann, Roland Cell Rep Article Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complex containing eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination. 2014-07-04 2014-07-10 /pmc/articles/PMC6813808/ /pubmed/25001285 http://dx.doi.org/10.1016/j.celrep.2014.04.058 Text en This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Article
Preis, Anne
Heuer, Andre
Barrio-Garcia, Clara
Hauser, Andreas
Eyler, Daniel E.
Berninghausen, Otto
Green, Rachel
Becker, Thomas
Beckmann, Roland
Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1
title Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1
title_full Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1
title_fullStr Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1
title_full_unstemmed Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1
title_short Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1
title_sort cryoelectron microscopic structures of eukaryotic translation termination complexes containing erf1-erf3 or erf1-abce1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6813808/
https://www.ncbi.nlm.nih.gov/pubmed/25001285
http://dx.doi.org/10.1016/j.celrep.2014.04.058
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