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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-2-14
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pubmed:abstractText |
Guide RNAs (gRNAs) are small RNAs that provide specificity for uridine addition and deletion during mRNA editing in trypanosomes. Terminal uridylyl transferase (TUTase) adds uridines to pre-mRNAs during RNA editing and adds a poly(U) tail to the 3' end of gRNAs. The poly(U) tail may stabilize the association of gRNAs with cognate mRNA during editing. Both TUTase and gRNAs associate with two ribonucleoprotein complexes, I (19S) and II (35S to 40S). Complex II is believed to be the fully assembled active editing complex, since it contains pre-edited mRNA and enzymes thought necessary for editing. Purification of TUTase from mitochondrial extracts resulted in the identification of two chromatographically distinct TUTase activities. Stable single-uridine addition to different substrate RNAs is performed by the 19S complex, despite the presence of a uridine-specific 3' exonuclease within this complex. Multiple uridines are added to substrate RNAs by a 10S particle that may be an unstable subunit of complex I lacking the uridine-specific 3' exonuclease. Multiple uridines could be stably added onto gRNAs by complex I when the cognate mRNA is present. We propose a model in which the purine-rich region of the cognate mRNA protects the uridine tail from a uridine exonuclease activity that is present within the complex. To test this model, we have mutated the purine-rich region of the pre-mRNA to abolish base-pairing interaction with the poly(U) tail of the gRNA. This RNA fails to protect the uridine tail of the gRNA from exoribonucleolytic trimming and is consistent with a role for the purine-rich region of the mRNA in gRNA maturation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1330537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1375322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1465424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1688737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1694178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1695552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-1719373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-2437529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-2438049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-6269049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-7512500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-7535769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-7667084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-8601307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-8657114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-8703045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-8754859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-8799125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-881656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-8978701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9016513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9108545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9160507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9175474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9233816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9271415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9380494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9422514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10629045-9889273
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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/Poly U,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Guide,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/UTP-RNA uridylyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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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 |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
883-91
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10629045-Animals,
pubmed-meshheading:10629045-Base Sequence,
pubmed-meshheading:10629045-Mitochondria,
pubmed-meshheading:10629045-Molecular Sequence Data,
pubmed-meshheading:10629045-Poly U,
pubmed-meshheading:10629045-RNA, Guide,
pubmed-meshheading:10629045-RNA, Messenger,
pubmed-meshheading:10629045-RNA, Protozoan,
pubmed-meshheading:10629045-RNA Editing,
pubmed-meshheading:10629045-RNA Nucleotidyltransferases,
pubmed-meshheading:10629045-RNA Precursors,
pubmed-meshheading:10629045-RNA Processing, Post-Transcriptional,
pubmed-meshheading:10629045-Ribonucleoproteins,
pubmed-meshheading:10629045-Trypanosoma brucei brucei
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pubmed:year |
2000
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pubmed:articleTitle |
Trypanosoma brucei guide RNA poly(U) tail formation is stabilized by cognate mRNA.
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pubmed:affiliation |
Department of Biochemistry, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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