Translation Initiation Factor eIF3b Contains a Nine-Bladed β-Propeller and Interacts with the 40S Ribosomal Subunit

被引：29
|
作者：
Liu, Yi [1 ]
Neumann, Piotr [1 ]
Kuhle, Bernhard [1 ]
Monecke, Thomas [1 ]
Schell, Stephanie [2 ]
Chari, Ashwin [2 ]
Ficner, Ralf [1 ]
机构：
[1] Univ Gottingen, GZMB, Inst Microbiol & Genet, Dept Mol Struct Biol, D-37077 Gottingen, Germany
[2] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany
来源：
STRUCTURE | 2014年 / 22卷 / 06期
关键词：
RNA RECOGNITION MOTIF; COMPLEX; BINDING; ARCHITECTURE; RECRUITMENT; INSIGHTS; SYSTEM; NIP1/C; PRT1;
D O I：
10.1016/j.str.2014.03.010
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The multisubunit eukaryotic translation initiation factor 3, among which the subunit b (eIF3b) is a major scaffold protein, plays essential roles in protein synthesis. Here, we report the crystal structure of the WD40 domain of Chaetomium thermophilum eIF3b, revealing a nine-bladed beta-propeller fold. Sequence analysis indicates that this propeller architecture is common to all eIF3b orthologs. Revisiting the cryo-electron microscopy (cryo-EM) map of the 43S preinitiation complex suggests an interaction of the eIF3b with the 40S ribosomal subunit involving the ribosomal protein S9e and the 18S rRNA. This model is strongly supported by the direct binding of eIF3b to 40S ribosomes and to the isolated ribosomal protein rpS9e in vitro.
引用
收藏
页码：923 / 930
页数：8
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