RDE-1 (RNAi-DEfective 1) is a primary Argonaute protein required for RNA-mediated interference (RNAi) in Caenorhabditis elegans. The rde-1 gene locus was first characterized in C. elegans mutants resistant to RNAi, and is a member of a highly conserved Piwi gene family that includes plant, Drosophila, and vertebrate homologs. [1]

1999年10月15日 · Two loci, rde-1 and rde-4, are defined by mutants strongly resistant to RNAi but with no obvious defects in growth or development. We show that rde-1 is a member of the piwi/sting/argonaute/zwille/eIF2C gene family conserved from plants to vertebrates.

Our results suggest distinct roles for RDE-1 and RDE-4 in the interference process. Although null mutants lacking rde-1 show no phenotypic response to dsRNA, the amount of siRNAs generated from an injected dsRNA trigger was comparable to that of wild-type.

2019年2月20日 · Here we constructed a germline-specific RNAi strain by combining an indel mutation of rde-1, which encodes an Argonaute protein that functions cell autonomously to ensure RNAi efficiency,...

AGO1, QDE-2 and RDE-1 are related proteins required for post-transcriptional gene silencing in plants, quelling in fungi and RNA interference in animals. RNA interference: traveling in the cell and gaining functions? Heriberto Cerutti, in Trends in Genetics, 2003.

RDE-1 activity is rescued in adult epidermal tissues, making animals RNAi-deficient except for hypodermal (skin) tissues from the young adult stage.

2009年1月18日 · Here we show that RNase H activity of RDE-1 is required only for efficient removal of the passenger strand of the siRNA duplex and not for triggering the silencing response at the target-mRNA...

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For example, rde-1 mutants are completely resistant to RNAi in all tissues (Tabara et al., 1999), but tissue-specific expression of rde-1 has been used to rescue RNAi in intestinal, muscle, neuronal, and hypodermal tissues (Espelt et al., 2005, Qadota et al., 2007, Firnhaber and Hammerlund, 2013).

2002年6月28日 · 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.