PMID:14508492

Citation	Caudy, AA, Ketting, RF, Hammond, SM, Denli, AM, Bathoorn, AM, Tops, BB, Silva, JM, Myers, MM, Hannon, GJ and Plasterk, RH (2003) A micrococcal nuclease homologue in RNAi effector complexes. Nature 425:411-4
Abstract	RNA interference (RNAi) regulates gene expression by the cleavage of messenger RNA, by mRNA degradation and by preventing protein synthesis. These effects are mediated by a ribonucleoprotein complex known as RISC (RNA-induced silencing complex). We have previously identified four Drosophila components (short interfering RNAs, Argonaute 2 (ref. 2), VIG and FXR) of a RISC enzyme that degrades specific mRNAs in response to a double-stranded-RNA trigger. Here we show that Tudor-SN (tudor staphylococcal nuclease)--a protein containing five staphylococcal/micrococcal nuclease domains and a tudor domain--is a component of the RISC enzyme in Caenorhabditis elegans, Drosophila and mammals. Although Tudor-SN contains non-canonical active-site sequences, we show that purified Tudor-SN exhibits nuclease activity similar to that of other staphylococcal nucleases. Notably, both purified Tudor-SN and RISC are inhibited by a specific competitive inhibitor of micrococcal nuclease. Tudor-SN is the first RISC subunit to be identified that contains a recognizable nuclease domain, and could therefore contribute to the RNA degradation observed in RNAi.
Links	PubMed Online version:10.1038/nature01956
Keywords	Animals; Binding Sites; Caenorhabditis elegans/enzymology; Drosophila melanogaster/enzymology; Macromolecular Substances; Micrococcal Nuclease/chemistry; Micrococcal Nuclease/isolation & purification; Micrococcal Nuclease/metabolism; Protein Structure, Tertiary; RNA Interference; RNA Processing, Post-Transcriptional; RNA-Induced Silencing Complex/chemistry; RNA-Induced Silencing Complex/metabolism
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