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.; Mielke, T.; Spahn, C. M. T.

doi:10.1038/nsmb.2859

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

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http://www.ncbi.nlm.nih.gov/pubmed/25064512
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引用

Yamamoto, H., Unbehaun, A., Loerke, J., Behrmann, E., Collier, M., Burger, J., Mielke, T., & Spahn, C. M. T. (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.

引用: https://hdl.handle.net/11858/00-001M-0000-0028-636A-A

要旨

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.