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

Becker, T., Armache, J. P., Jarasch, A., Anger, A. M., Villa, E., Sieber, H., et al. (2011). Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome. Nature Structural & Molecular Biology, 18(6), 715-20. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/21623367 http://www.nature.com/nsmb/journal/v18/n6/pdf/nsmb.2057.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-78EE-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-78EF-7
Genre: Journal Article

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 Creators:
Becker, T., Author
Armache, J. P., Author
Jarasch, A., Author
Anger, A. M., Author
Villa, E., Author
Sieber, H., Author
Motaal, B. A., Author
Mielke, T.1, Author              
Berninghausen, O., Author
Beckmann, R., Author
Affiliations:
1Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: Cell Cycle Proteins/chemistry/metabolism/*ultrastructure; Cryoelectron Microscopy; Endoribonucleases/chemistry/metabolism/*ultrastructure; GTP-Binding Proteins/chemistry/metabolism/*ultrastructure; HSP70 Heat-Shock Proteins/chemistry/metabolism/*ultrastructure; Models, Molecular; Peptide Elongation Factors/chemistry/metabolism/*ultrastructure; Protein Binding; RNA Stability; RNA, Messenger/chemistry/metabolism; Ribosomes/chemistry/metabolism/*ultrastructure; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/chemistry/metabolism/*ultrastructure
 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.

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 Dates: 2011
 Publication Status: Published in print
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Title: Nature Structural & Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 18 (6) Sequence Number: - Start / End Page: 715 - 20 Identifier: ISSN: 1545-9985 (Electronic) 1545-9985 (Linking)