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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
2004-11-15
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pubmed:abstractText |
In all trypanosomatids, trans splicing of the spliced leader (SL) RNA is a required step in the maturation of all nucleus-derived mRNAs. The SL RNA is transcribed with an oligo-U 3' extension that is removed prior to trans splicing. Here we report the identification and characterization of a nonexosomal, 3'-->5' exonuclease required for SL RNA 3'-end formation in Trypanosoma brucei. We named this enzyme SNIP (for snRNA incomplete 3' processing). The central 158-amino-acid domain of SNIP is related to the exonuclease III (ExoIII) domain of the 3'-->5' proofreading epsilon subunit of Escherichia coli DNA polymerase III holoenzyme. SNIP had a preference for oligo(U) 3' extensions in vitro. RNA interference-mediated knockdown of SNIP resulted in a growth defect and correlated with the accumulation of one- to two- nucleotide 3' extensions of SL RNA, U2 and U4 snRNAs, a five-nucleotide extension of 5S rRNA, and the destabilization of U3 snoRNA and U2 snRNA. SNIP-green fluorescent protein localized to the nucleoplasm, and substrate SL RNA derived from SNIP knockdown cells showed wild-type cap 4 modification, indicating that SNIP acts on SL RNA after cytosolic trafficking. Since the primary SL RNA transcript was not the accumulating species in SNIP knockdown cells, SL RNA 3'-end formation is a multistep process in which SNIP provides the ultimate 3'-end polishing. We speculate that SNIP is part of an organized nucleoplasmic machinery responsible for processing of SL RNA.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-10215027,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-10383448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-10571176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-10716935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-11013266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-11279235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-11447124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-11719056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-11868988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-12684371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-12746436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-12821657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-12878606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-14532264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-14871954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-15212793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-1549111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-2411548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-9668037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-9891092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15542846-9927735
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Kinetoplast,
http://linkedlifedata.com/resource/pubmed/chemical/Exonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 5S,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Spliced Leader,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10390-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15542846-Animals,
pubmed-meshheading:15542846-Cell Line,
pubmed-meshheading:15542846-Cell Nucleus,
pubmed-meshheading:15542846-Cells, Cultured,
pubmed-meshheading:15542846-Cloning, Molecular,
pubmed-meshheading:15542846-Cytoplasm,
pubmed-meshheading:15542846-Cytosol,
pubmed-meshheading:15542846-DNA, Kinetoplast,
pubmed-meshheading:15542846-Escherichia coli,
pubmed-meshheading:15542846-Exonucleases,
pubmed-meshheading:15542846-Green Fluorescent Proteins,
pubmed-meshheading:15542846-Microscopy, Fluorescence,
pubmed-meshheading:15542846-Models, Biological,
pubmed-meshheading:15542846-Phenotype,
pubmed-meshheading:15542846-Plasmids,
pubmed-meshheading:15542846-Protein Structure, Tertiary,
pubmed-meshheading:15542846-RNA,
pubmed-meshheading:15542846-RNA, Ribosomal, 5S,
pubmed-meshheading:15542846-RNA, Spliced Leader,
pubmed-meshheading:15542846-RNA Interference,
pubmed-meshheading:15542846-RNA Precursors,
pubmed-meshheading:15542846-RNA Splicing,
pubmed-meshheading:15542846-Time Factors,
pubmed-meshheading:15542846-Transfection,
pubmed-meshheading:15542846-Trypanosoma brucei brucei
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pubmed:year |
2004
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pubmed:articleTitle |
3'-End polishing of the kinetoplastid spliced leader RNA is performed by SNIP, a 3'-->5' exonuclease with a Motley assortment of small RNA substrates.
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pubmed:affiliation |
Department of Microbiology, Immunology, and Molecular Genetics, University of California at Los Angeles, 609 Charles E. Young Dr. East, Los Angeles, CA 90095-1489, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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