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The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex.


ABSTRACT: The translation, localization, and degradation of cytoplasmic mRNAs are controlled by the formation and rearrangement of their mRNPs. The conserved Ded1/DDX3 DEAD-box protein functions in an unknown manner to affect both translation initiation and repression. We demonstrate that Ded1 first functions by directly interacting with eIF4G to assemble a Ded1-mRNA-eIF4F complex, which accumulates in stress granules. After ATP hydrolysis by Ded1, the mRNP exits stress granules and completes translation initiation. Thus, Ded1 functions both as a repressor of translation, by assembling an mRNP stalled in translation initiation, and as an ATP-dependent activator of translation, by resolving the stalled mRNP. These results identify Ded1 as a translation initiation factor that assembles and remodels an intermediate complex in translation initiation.

SUBMITTER: Hilliker A 

PROVIDER: S-EPMC3268518 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

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The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex.

Hilliker Angela A   Gao Zhaofeng Z   Jankowsky Eckhard E   Parker Roy R  

Molecular cell 20110901 6


The translation, localization, and degradation of cytoplasmic mRNAs are controlled by the formation and rearrangement of their mRNPs. The conserved Ded1/DDX3 DEAD-box protein functions in an unknown manner to affect both translation initiation and repression. We demonstrate that Ded1 first functions by directly interacting with eIF4G to assemble a Ded1-mRNA-eIF4F complex, which accumulates in stress granules. After ATP hydrolysis by Ded1, the mRNP exits stress granules and completes translation  ...[more]

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