The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo

被引：125

作者：

Valásek, L ^{[1
]}

Mathew, AA ^{[1
]}

Shin, BS ^{[1
]}

Nielsen, KH ^{[1
]}

Szamecz, B ^{[1
]}

Hinnebusch, AG ^{[1
]}

机构：

[1] NICHHD, Lab Gene Regulat & Dev, Bethesda, MD 20892 USA

来源：

GENES & DEVELOPMENT | 2003年 / 17卷 / 06期

关键词：

eukaryotic translation initiation factor (eIf); multifactor complex (MFC); translational control; protein synthesis; 40S ribosome binding; TIF32/NIP1;

D O I：

10.1101/gad.1065403

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Initiation factor 3 (eIF3) forms a multifactor complex (MFC) with eIF1, eIF2, and eIF5 that stimulates Met-tRNA(i)(Met) binding to 40S ribosomes and promotes scanning or AUG recognition. We have previously characterized MFC subcomplexes produced in vivo from affinity-tagged eIF3 subunits lacking discrete binding domains for other MFC components. Here we asked whether these subcomplexes can bind to 40S ribosomes in vivo. We found that the N-and C-terminal domains of NIP1/eIF3c, the N-and C-terminal domains of TIF32/eIF3a, and eIF5 have critical functions in 40S binding, with eIF5 and the TIF32-CTD performing redundant functions. The TIF32-CTD interacted in vitro with helices 16-18 of domain I in 18S rRNA, and the TIF32-NTD and NIP1 interacted with 40S protein RPSOA. These results suggest that eIF3 binds to the solvent side of the 40S subunit in a way that provides access to the interface side for the two eIF3 segments (NIP1-NTD and TIF32-CTD) that interact with eIF1, eIF5, and the eIF2/GTP/Met-tRNA(i)(Met) ternary complex.

引用

页码：786 / 799

页数：14

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