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

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.

Pubmed ID: 21925384


  • Hilliker A
  • Gao Z
  • Jankowsky E
  • Parker R


Molecular cell

Publication Data

September 16, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM067700
  • Agency: NIGMS NIH HHS, Id: GM45443
  • Agency: NIGMS NIH HHS, Id: R37 GM045443
  • Agency: NIGMS NIH HHS, Id: R37 GM045443-21
  • Agency: Howard Hughes Medical Institute, Id:

Mesh Terms

  • Adenosine Triphosphate
  • Amino Acid Sequence
  • Cytoplasmic Granules
  • DEAD-box RNA Helicases
  • Eukaryotic Initiation Factor-4F
  • Eukaryotic Initiation Factor-4G
  • Gene Expression Regulation
  • Models, Genetic
  • Molecular Sequence Data
  • Protein Biosynthesis
  • RNA, Messenger
  • Ribonucleoproteins
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment