Hammond, S. M., Boettcher, S., Caudy, A. A., Kobayashi, R., Hannon, G. J. (August 2001) Argonaute2, a link between genetic and biochemical analyses of RNAi. Science, 293 (5532). pp. 1146-1150. ISSN 0036-8075
Abstract
Double-stranded RNA induces potent and specific gene silencing through a process referred to as RNA interference (RNAi) or posttranscriptional gene silencing (PTGS). RNAi is mediated by RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys messenger RNAs homologous to the silencing trigger. RISC is known to contain short RNAs (similar to 22 nucleotides) derived from the double-stranded RNA trigger, but the protein components of this activity are unknown. Here, we report the biochemical purification of the RNAi effector nuclease from cultured Drosophila cells. The active fraction contains a ribonucleoprotein complex of similar to 500 kilodaltons. Protein microsequencing reveals that one constituent of this complex is a member of the Argonaute family of proteins, which are essential for gene silencing in Caenorhabditis elegans, Neurospora, and Arabidopsis. This observation begins the process of forging links between genetic analysis of RNAi from diverse organisms and the biochemical model of RNAi that is emerging from Drosophila in vitro systems.
Item Type: | Paper |
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Uncontrolled Keywords: | DOUBLE-STRANDED-RNA C-ELEGANS MESSENGER-RNA INTERFERENCE ARABIDOPSIS POLYMERASE HELICASE NEUROSPORA TRANSGENE PROTEINS |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > RNAi bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > argonaute proteins |
CSHL Authors: | |
Communities: | CSHL labs > Hannon lab CSHL labs > Kobayashi lab School of Biological Sciences > Publications |
Depositing User: | Matt Covey |
Date: | August 2001 |
Date Deposited: | 22 Jan 2014 19:25 |
Last Modified: | 19 Sep 2014 13:49 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/29242 |
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