Source:http://linkedlifedata.com/resource/pubmed/id/14508492
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6956
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pubmed:dateCreated |
2003-9-25
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1476-4687
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pubmed:author |
pubmed-author:BathoornAnja M PAM,
pubmed-author:CaudyAmy AAA,
pubmed-author:DenliAhmet MAM,
pubmed-author:HammondScott MSM,
pubmed-author:HannonGregory JGJ,
pubmed-author:KettingRené FRF,
pubmed-author:MyersMike MMM,
pubmed-author:PlasterkRonald H ARH,
pubmed-author:SilvaJose MJM,
pubmed-author:TopsBastiaan B JBB
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pubmed:issnType |
Electronic
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pubmed:day |
25
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pubmed:volume |
425
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
411-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14508492-Animals,
pubmed-meshheading:14508492-Binding Sites,
pubmed-meshheading:14508492-Caenorhabditis elegans,
pubmed-meshheading:14508492-Drosophila melanogaster,
pubmed-meshheading:14508492-Macromolecular Substances,
pubmed-meshheading:14508492-Micrococcal Nuclease,
pubmed-meshheading:14508492-Protein Structure, Tertiary,
pubmed-meshheading:14508492-RNA Interference,
pubmed-meshheading:14508492-RNA Processing, Post-Transcriptional,
pubmed-meshheading:14508492-RNA-Induced Silencing Complex
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pubmed:year |
2003
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pubmed:articleTitle |
A micrococcal nuclease homologue in RNAi effector complexes.
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pubmed:affiliation |
Cold Spring Harbor Laboratory, Watson School of Biological Sciences, 1 Bungtown Road, Cold Spring Harbor, New York 11724, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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