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  Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated Cricket Paralysis Virus IRES

Muhs, M., Hilal, T., Mielke, T., Skabkin, M. A., Sanbonmatsu, K. Y., Pestova, T. V., et al. (2015). Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated Cricket Paralysis Virus IRES. Molecular Cell, 57(3), 422-432. doi:10.1016/j.molcel.2014.12.016.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A9AE-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A9AF-5
Genre: Journal Article

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 Creators:
Muhs, Margita1, Author
Hilal, Tarek 1, Author
Mielke, Thorsten1, 2, Author              
Skabkin, Maxim A. 3, Author
Sanbonmatsu, Karissa Y. 4, 5, Author
Pestova, Tatyana V.3, Author
Spahn, Christian M. T. 1, Author
Affiliations:
1Institut für Medizinische Physik und Biophysik, Charite – 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              
3Department of Cell Biology, SUNY Downstate Medical Center, Brooklyn, NY 11203, USA, ou_persistent22              
4Theoretical Biology and Biophysics Group, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA, ou_persistent22              
5New Mexico Consortium, 4200 West Jemez Road, Suite 301, Los Alamos, NM 87544, USA, ou_persistent22              

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 Abstract: The cricket paralysis virus (CrPV) uses an internal ribosomal entry site (IRES) to hijack the ribosome. In a remarkable RNA-based mechanism involving neither initiation factor nor initiator tRNA, the CrPV IRES jumpstarts translation in the elongation phase from the ribosomal A site. Here, we present cryoelectron microscopy (cryo-EM) maps of 80S⋅CrPV-STOP ⋅ eRF1 ⋅ eRF3 ⋅ GMPPNP and 80S⋅CrPV-STOP ⋅ eRF1 complexes, revealing a previously unseen binding state of the IRES and directly rationalizing that an eEF2-dependent translocation of the IRES is required to allow the first A-site occupation. During this unusual translocation event, the IRES undergoes a pronounced conformational change to a more stretched conformation. At the same time, our structural analysis provides information about the binding modes of eRF1 ⋅ eRF3 ⋅ GMPPNP and eRF1 in a minimal system. It shows that neither eRF3 nor ABCE1 are required for the active conformation of eRF1 at the intersection between eukaryotic termination and recycling.

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Language(s): eng - English
 Dates: 2015-01-152015-02-05
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.12.016
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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 57 (3) Sequence Number: - Start / End Page: 422 - 432 Identifier: ISSN: 1097-2765
CoNE: /journals/resource/954925610929