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  Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA

Yamamoto, H., Unbehaun, A., Loerke, J., Behrmann, E., Collier, M., Bürger, J., et al. (2014). Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA. Nature Structural and Molecular Biology, 21(8), 721-727. doi:10.1038/nsmb.2859.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-B244-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-B245-E
Genre: Journal Article

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 Creators:
Yamamoto, H., Author
Unbehaun, A., Author
Loerke, J., Author
Behrmann, E.1, Author              
Collier, M., Author
Bürger, Jörg2, Author              
Mielke, Thorsten2, Author              
Spahn, C. M. T., Author
Affiliations:
1Research Group Structural Dynamics of Proteins, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_2173687              
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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Free keywords: The universally conserved eukaryotic initiation factor (eIF) 5B, a translational GTPase, is essential for canonical translation initiation. It is also required for initiation facilitated by the internal ribosomal entry site (IRES) of hepatitis C virus (HCV) RNA. eIF5B promotes joining of 60S ribosomal subunits to 40S ribosomal subunits bound by initiator tRNA (Met-tRNAi(Met)). However, the exact molecular mechanism by which eIF5B acts has not been established. Here we present cryo-EM reconstructions of the mammalian 80S-HCV-IRES-Met-tRNAi(Met)-eIF5B-GMPPNP complex. We obtained two substates distinguished by the rotational state of the ribosomal subunits and the configuration of initiator tRNA in the peptidyl (P) site. Accordingly, a combination of conformational changes in the 80S ribosome and in initiator tRNA facilitates binding of the Met-tRNAi(Met) to the 60S P site and redefines the role of eIF5B as a tRNA-reorientation factor.
 Abstract: The universally conserved eukaryotic initiation factor (eIF) 5B, a translational GTPase, is essential for canonical translation initiation. It is also required for initiation facilitated by the internal ribosomal entry site (IRES) of hepatitis C virus (HCV) RNA. eIF5B promotes joining of 60S ribosomal subunits to 40S ribosomal subunits bound by initiator tRNA (Met-tRNAi(Met)). However, the exact molecular mechanism by which eIF5B acts has not been established. Here we present cryo-EM reconstructions of the mammalian 80S-HCV-IRES-Met-tRNAi(Met)-eIF5B-GMPPNP complex. We obtained two substates distinguished by the rotational state of the ribosomal subunits and the configuration of initiator tRNA in the peptidyl (P) site. Accordingly, a combination of conformational changes in the 80S ribosome and in initiator tRNA facilitates binding of the Met-tRNAi(Met) to the 60S P site and redefines the role of eIF5B as a tRNA-reorientation factor.

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Language(s): eng - English
 Dates: 2014-06-202014-07-272014-08
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2859
 Degree: -

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Title: Nature Structural and Molecular Biology
  Other : Nature Struct Biol
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 21 (8) Sequence Number: - Start / End Page: 721 - 727 Identifier: ISSN: 1545-9993
CoNE: /journals/resource/954925603763