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Article

Structural Roles for Human Translation Factor eIF3 in Initiation of Protein Synthesis

1 Dec 2005

Abstract excerpt

Protein synthesis in mammalian cells requires initiation factor eIF3, a approximately 750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5'-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that eIF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5'-cap binding complex...

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Identifiers

PMID: 16322461
DOI: 10.1126/science.1118977

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Structural Roles for Human Translation Factor eIF3 in Initiation of Protein SynthesisPMID 16322461Read ↗

Two RNA-binding motifs in eIF3 direct HCV IRES-dependent translation.Semantic proximity Read ↗

Coordinated assembly of human translation initiation complexes by the hepatitis C virus internal ribosome entry site RNASemantic proximity Read ↗

Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.Semantic proximity Read ↗

Translation initiation by the hepatitis C virus IRES requires eIF1A and ribosomal complex remodelingSemantic proximity Read ↗

Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolutionSemantic proximity Read ↗

Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunitSemantic proximity Read ↗

A structural inventory of native ribosomal ABCE1‐43S pre‐initiation complexesSemantic proximity Read ↗

A conserved RNA structure within the HCV IRES eIF3-binding siteSemantic proximity Read ↗

Structural and Functional Insights into Human Re-initiation Complexes.Semantic proximity Read ↗

Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation.Semantic proximity Read ↗

Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly.Semantic proximity Read ↗

Conservation and diversity in the structure of translation initiation factor EIF3 from humans and yeast.Semantic proximity Read ↗

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