Coupling between the DEAD-box RNA helicases Ded1p and eIF4A

被引：47

作者：

Gao, Zhaofeng ^{[1
,2
]}

Putnam, Andrea A. ^{[1
,2
]}

Bowers, Heath ^{[1
,2
]}

Guenther, Ulf-Peter ^{[1
,2
]}

Ye, Xuan ^{[1
,2
]}

Kindsfather, Audrey ^{[3
]}

Hilliker, Angela K. ^{[3
]}

Jankowsky, Eckhard ^{[1
,2
]}

机构：

[1] Case Western Reserve Univ, Sch Med, Ctr RNA Mol Biol, Cleveland, OH 44106 USA

[2] Case Western Reserve Univ, Sch Med, Dept Biochem, Cleveland, OH 44106 USA

[3] Univ Richmond, Dept Biol, Richmond, VA USA

来源：

ELIFE | 2016年 / 5卷

关键词：

INDEPENDENT-MUTAGENESIS SLIM; TRANSLATION INITIATION; SACCHAROMYCES-CEREVISIAE; PROTEIN DED1; DEPENDENT TRANSLATION; SOMATIC MUTATIONS; GENE-EXPRESSION; MESSENGER-RNAS; KINETIC-DATA; IN-VIVO;

D O I：

10.7554/eLife.16408

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Eukaryotic translation initiation involves two conserved DEAD-box RNA helicases, eIF4A and Ded1p. Here we show that S. cerevisiae eIF4A and Ded1p directly interact with each other and simultaneously with the scaffolding protein eIF4G. We delineate a comprehensive thermodynamic framework for the interactions between Ded1p, eIF4A, eIF4G, RNA and ATP, which indicates that eIF4A, with and without eIF4G, acts as modulator for activity and substrate preferences of Ded1p, which is the RNA remodeling unit in all complexes. Our results reveal and characterize an unexpected interdependence between the two RNA helicases and eIF4G, and suggest that Ded1p is an integral part of eIF4F, the complex comprising eIF4G, eIF4A, and eIF4E.

引用

页数：59

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