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 RIS Download
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