Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome

Thomas Becker; Jean Paul Armache; Alexander Jarasch; Andreas M. Anger; Elizabeth Villa; Heidemarie Sieber; Basma Abdel Motaal; Thorsten Mielke; Otto Berninghausen; Roland Beckmann

doi:10.1038/nsmb.2057

Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome

Thomas Becker, Jean Paul Armache, Alexander Jarasch, Andreas M. Anger, Elizabeth Villa, Heidemarie Sieber, Basma Abdel Motaal, Thorsten Mielke, Otto Berninghausen, Roland Beckmann

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

139 Scopus citations

Abstract

No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.

Original language	English (US)
Pages (from-to)	715-720
Number of pages	6
Journal	Nature Structural and Molecular Biology
Volume	18
Issue number	6
DOIs	https://doi.org/10.1038/nsmb.2057
State	Published - Jun 2011

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

Access to Document

10.1038/nsmb.2057

Cite this

@article{2da862b2ef0a4495828591008f254be3,

title = "Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome",

abstract = "No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.",

author = "Thomas Becker and Armache, {Jean Paul} and Alexander Jarasch and Anger, {Andreas M.} and Elizabeth Villa and Heidemarie Sieber and Motaal, {Basma Abdel} and Thorsten Mielke and Otto Berninghausen and Roland Beckmann",

year = "2011",

month = jun,

doi = "10.1038/nsmb.2057",

language = "English (US)",

volume = "18",

pages = "715--720",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Research",

number = "6",

}

TY - JOUR

T1 - Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome

AU - Becker, Thomas

AU - Armache, Jean Paul

AU - Jarasch, Alexander

AU - Anger, Andreas M.

AU - Villa, Elizabeth

AU - Sieber, Heidemarie

AU - Motaal, Basma Abdel

AU - Mielke, Thorsten

AU - Berninghausen, Otto

AU - Beckmann, Roland

PY - 2011/6

Y1 - 2011/6

N2 - No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.

AB - No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.

UR - http://www.scopus.com/inward/record.url?scp=79958809003&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79958809003&partnerID=8YFLogxK

U2 - 10.1038/nsmb.2057

DO - 10.1038/nsmb.2057

M3 - Article

C2 - 21623367

AN - SCOPUS:79958809003

SN - 1545-9993

VL - 18

SP - 715

EP - 720

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 6

ER -

Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this