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The dsRNA binding protein RDE-4 interacts with RDE-1, DCR-1, and a DExH-box helicase to direct RNAi in C. elegans.

Double-stranded (ds) RNA induces potent gene silencing, termed RNA interference (RNAi). At an early step in RNAi, an RNaseIII-related enzyme, Dicer (DCR-1), processes long-trigger dsRNA into small interfering RNAs (siRNAs). DCR-1 is also required for processing endogenous regulatory RNAs called miRNAs, but how DCR-1 recognizes its endogenous and foreign substrates is not yet understood. Here we show that the C. elegans RNAi pathway gene, rde-4, encodes a dsRNA binding protein that interacts during RNAi with RNA identical to the trigger dsRNA. RDE-4 protein also interacts in vivo with DCR-1, RDE-1, and a conserved DExH-box helicase. Our findings suggest a model in which RDE-4 and RDE-1 function together to detect and retain foreign dsRNA and to present this dsRNA to DCR-1 for processing.

Pubmed ID: 12110183

Authors

  • Tabara H
  • Yigit E
  • Siomi H
  • Mello CC

Journal

Cell

Publication Data

June 28, 2002

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM58800

Mesh Terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins
  • Cloning, Molecular
  • Conserved Sequence
  • DEAD-box RNA Helicases
  • Endoribonucleases
  • Gene Silencing
  • Helminth Proteins
  • Humans
  • Molecular Sequence Data
  • Peptide Mapping
  • Protein Binding
  • RNA Helicases
  • RNA, Double-Stranded
  • RNA, Messenger
  • RNA-Binding Proteins
  • Ribonuclease III
  • Sequence Homology, Amino Acid