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 journalArticle

112 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 languageEnglish (US)
Pages (from-to)715-720
Number of pages6
JournalNature Structural and Molecular Biology
Volume18
Issue number6
DOIs
StatePublished - Jun 1 2011

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome'. Together they form a unique fingerprint.

  • Cite this

    Becker, T., Armache, J. P., Jarasch, A., Anger, A. M., Villa, E., Sieber, H., Motaal, B. A., Mielke, T., Berninghausen, O., & Beckmann, R. (2011). Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome. Nature Structural and Molecular Biology, 18(6), 715-720. https://doi.org/10.1038/nsmb.2057