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Article

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

Nucleic acids research - 1 Mar 2012

Herrmannová Anna, Daujotyte Dalia, Yang Ji-Chun, Cuchalová Lucie, Gorrec Fabrice, Wagner Susan, Dányi István, Lukavsky Peter J, Valásek Leos Shivaya

Abstract excerpt

Translation initiation factor eIF3 acts as the key orchestrator of the canonical initiation pathway in eukaryotes, yet its structure is greatly unexplored. We report the 2.2 Å resolution crystal structure of the complex between the yeast seven-bladed β-propeller eIF3i/TIF34 and a C-terminal α-helix of eIF3b/PRT1, which reveals universally conserved interactions. Mutating these interactions displays severe growth...

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Identifiers

PMID: 22090426
DOI: 10.1093/nar/gkr765
PMCID: PMC3300007

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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