3ZWL

Structure of eukaryotic translation initiation factor eIF3i complex with eIF3b C-terminus (655-700)

3ZWL の概要

• エントリーDOI: 10.2210/pdb3zwl/pdb
• 分子名称: EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT I, EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B (3 entities in total)
• 機能のキーワード: translation
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm (Probable): P40217 P06103
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 94731.65

構造登録者

Daujotyte, D.,Lukavsky, P.J. (登録日: 2011-08-01, 公開日: 2011-10-05, 最終更新日: 2024-05-08)

主引用文献

Herrmannova, A.,Daujotyte, D.,Yang, J.C.,Cuchalova, L.,Gorrec, F.,Wagner, S.,Danyi, I.,Lukavsky, P.J.,Shivaya Valasek, L.
Structural Analysis of an Eif3 Subcomplex Reveals Conserved Interactions Required for a Stable and Proper Translation Pre-Initiation Complex Assembly.
Nucleic Acids Res., 40:2294-, 2012

PubMed Abstract: 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 defects and eliminates association of eIF3i/TIF34 and strikingly also eIF3g/TIF35 with eIF3 and 40S subunits in vivo. Unexpectedly, 40S-association of the remaining eIF3 subcomplex and eIF5 is likewise destabilized resulting in formation of aberrant pre-initiation complexes (PICs) containing eIF2 and eIF1, which critically compromises scanning arrest on mRNA at its AUG start codon suggesting that the contacts between mRNA and ribosomal decoding site are impaired. Remarkably, overexpression of eIF3g/TIF35 suppresses the leaky scanning and growth defects most probably by preventing these aberrant PICs to form. Leaky scanning is also partially suppressed by eIF1, one of the key regulators of AUG recognition, and its mutant sui1(G107R) but the mechanism differs. We conclude that the C-terminus of eIF3b/PRT1 orchestrates co-operative recruitment of eIF3i/TIF34 and eIF3g/TIF35 to the 40S subunit for a stable and proper assembly of 48S pre-initiation complexes necessary for stringent AUG recognition on mRNAs.

PubMed: 22090426
DOI: 10.1093/NAR/GKR765

実験手法

X-RAY DIFFRACTION (2.2 Å)