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, 109 (7), 861-71

The dsRNA Binding Protein RDE-4 Interacts With RDE-1, DCR-1, and a DExH-box Helicase to Direct RNAi in C. Elegans

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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

Hiroaki Tabara et al. Cell.

Abstract

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.

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