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  tRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis

Flis, J., Holm, M., Rundlet, E. J., Loerke, J., Hilal, T., Dabrowski, M., et al. (2018). tRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis. Cell Reports, 25(10): e7, pp. 2676-2688. doi:10.1016/j.celrep.2018.11.040.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-566D-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-566E-2
Genre: Journal Article

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 Creators:
Flis, Julia , Author
Holm, Mikael , Author
Rundlet, Emily J. , Author
Loerke, Justus , Author
Hilal, Tarek , Author
Dabrowski, Marylena , Author
Bürger, Jörg1, Author              
Mielke, Thorsten1, Author              
Blanchard, Scott C. , Author
Spahn, Christian M.T. , Author
Budkevich, Tatyana V. , Author
Affiliations:
1Microscopy 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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Free keywords: EF-G; cryo-EM; elongation factor eEF2; large-scale conformational changes; macromolecular machine; mammalian ribosome; smFRET; translation elongation; translocation
 Abstract: Translocation moves the tRNA2⋅mRNA module directionally through the ribosome during the elongation phase of protein synthesis. Although translocation is known to entail large conformational changes within both the ribosome and tRNA substrates, the orchestrated events that ensure the speed and fidelity of this critical aspect of the protein synthesis mechanism have not been fully elucidated. Here, we present three high-resolution structures of intermediates of translocation on the mammalian ribosome where, in contrast to bacteria, ribosomal complexes containing the translocase eEF2 and the complete tRNA2⋅mRNA module are trapped by the non-hydrolyzable GTP analog GMPPNP. Consistent with the observed structures, single-molecule imaging revealed that GTP hydrolysis principally facilitates rate-limiting, final steps of translocation, which are required for factor dissociation and which are differentially regulated in bacterial and mammalian systems by the rates of deacyl-tRNA dissociation from the E site.

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Language(s): eng - English
 Dates: 2018-12-04
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1016/j.celrep.2018.11.040
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Title: Cell Reports
Source Genre: Journal
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Publ. Info: Maryland Heights, MO : Cell Press
Pages: 13 Volume / Issue: 25 (10) Sequence Number: e7 Start / End Page: 2676 - 2688 Identifier: ISSN: 2211-1247
CoNE: https://pure.mpg.de/cone/journals/resource/2211-1247