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| Title | Two RNA-binding motifs in eIF3 direct HCV IRES-dependent translation. |
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| Journal, issue, pages | Nucleic Acids Res, Vol. 41, Issue 15, Page 7512-7521, Year 2013 |
| Publish date | Jun 13, 2013 |
 Authors | Chaomin Sun / Jordi Querol-Audí / Stefanie A Mortimer / Ernesto Arias-Palomo / Jennifer A Doudna / Eva Nogales / Jamie H D Cate /  |
| PubMed Abstract | The initiation of protein synthesis plays an essential regulatory role in human biology. At the center of the initiation pathway, the 13-subunit eukaryotic translation initiation factor 3 (eIF3) ...The initiation of protein synthesis plays an essential regulatory role in human biology. At the center of the initiation pathway, the 13-subunit eukaryotic translation initiation factor 3 (eIF3) controls access of other initiation factors and mRNA to the ribosome by unknown mechanisms. Using electron microscopy (EM), bioinformatics and biochemical experiments, we identify two highly conserved RNA-binding motifs in eIF3 that direct translation initiation from the hepatitis C virus internal ribosome entry site (HCV IRES) RNA. Mutations in the RNA-binding motif of subunit eIF3a weaken eIF3 binding to the HCV IRES and the 40S ribosomal subunit, thereby suppressing eIF2-dependent recognition of the start codon. Mutations in the eIF3c RNA-binding motif also reduce 40S ribosomal subunit binding to eIF3, and inhibit eIF5B-dependent steps downstream of start codon recognition. These results provide the first connection between the structure of the central translation initiation factor eIF3 and recognition of the HCV genomic RNA start codon, molecular interactions that likely extend to the human transcriptome. |
 External links | Nucleic Acids Res / PubMed:23766293 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 20.0 Å |
| Structure data |  EMDB-2198:  EMDB-2199: |
| Source |
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Homo sapiens (human)
Hepatitis C virus