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  Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution

Hilal, T., Yamamoto, H., Loerke, J., Bürger, J., Mielke, T., & Spahn, C. M. T. (2016). Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution. Nature Communications, 7: 7:13521. doi:10.1038/ncomms13521.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2432-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2433-6
Genre: Journal Article

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Hilal, Tarek 1, Author
Yamamoto, Hiroshi 1, Author
Loerke, Justus 1, Author
Bürger, Jörg1, 2, Author              
Mielke, Thorsten2, Author              
Spahn, Christian M. T. , Author
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1 Institut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany, ou_persistent22              
2Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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 Abstract: The surveillance of mRNA translation is imperative for homeostasis. Monitoring the integrity of the message is essential, as the translation of aberrant mRNAs leads to stalling of the translational machinery. During ribosomal rescue, arrested ribosomes are specifically recognized by the conserved eukaryotic proteins Dom34 and Hbs1, to initiate their recycling. Here we solve the structure of Dom34 and Hbs1 bound to a yeast ribosome programmed with a nonstop mRNA at 3.3 Å resolution using cryo-electron microscopy. The structure shows that Domain N of Dom34 is inserted into the upstream mRNA-binding groove via direct stacking interactions with conserved nucleotides of 18S rRNA. It senses the absence of mRNA at the A-site and part of the mRNA entry channel by direct competition. Thus, our analysis establishes the structural foundation for the recognition of aberrantly stalled 80S ribosomes by the Dom34·Hbs1·GTP complex during Dom34-mediated mRNA surveillance pathways.

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 Dates: 2016-10-112016-12-20
 Publication Status: Published online
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 Identifiers: DOI: 10.1038/ncomms13521
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 7 Sequence Number: 7:13521 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: /journals/resource/2041-1723