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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., Burger, J., et al. (2014). Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA. Nature structural & molecular biology, 21(8), 721-7. doi:10.1038/nsmb.2859.

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Yamamoto, H., Author
Unbehaun, A., Author
Loerke, J., Author
Behrmann, E.1, Author
Collier, M., Author
Burger, J., Author
Mielke, T., Author
Spahn, C. M. T., Author
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1External Organizations, ou_persistent22              

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 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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 Dates: 2014
 Publication Status: Issued
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 Identifiers: Other: 25064512
DOI: 10.1038/nsmb.2859
ISSN: 1545-9985 (Electronic)
ISSN: 1545-9985 (Linking)
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Title: Nature structural & molecular biology
  Alternative Title : Nat. Struct. Mol. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 21 (8) Sequence Number: - Start / End Page: 721 - 7 Identifier: -