A micrococcal nuclease homologue in RNAi effector complexes

Caudy, A. A., Ketting, R. F., Hammond, S. M., Denli, A. M., Bathoorn, A. M. P., Tops, B. B. J., Silva, J. M., Myers, M. M., Hannon, G. J., Plasterk, R. H. A. (2003) A micrococcal nuclease homologue in RNAi effector complexes. Nature, 425 (6956). pp. 411-414. ISSN 00280836 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/14508492
DOI: 10.1038/nature01956

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 ribonucleo-protein 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.

Item Type: Paper
Uncontrolled Keywords: Biosynthesis Degradation Enzymes RNA Protein synthesis Microorganisms bacterial enzyme ribonucleoprotein RNA derivative rna induced silencing complex protein small interfering RNA tudor staphylococcal nuclease unclassified drug animal cell article Caenorhabditis elegans competitive inhibition controlled study Drosophila effector cell enzyme active site enzyme activity enzyme analysis enzyme inhibition enzyme specificity gene expression regulation mammal Micrococcus nonhuman priority journal protein domain protein purification RNA analysis RNA degradation sequence analysis Staphylococcus Animals Binding Sites Drosophila melanogaster Macromolecular Substances Micrococcal Nuclease Protein Structure, Tertiary RNA Interference RNA Processing, Post-Transcriptional RNA-Induced Silencing Complex Animalia Bacteria (microorganisms) Caenorhabditis Mammalia
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > RNAi
CSHL Authors:
Communities: CSHL labs > Hannon lab
Watson School > Publications
Depositing User: Matt Covey
Date: 2003
Date Deposited: 09 Jan 2013 16:50
Last Modified: 19 Sep 2014 14:35
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26459

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