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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2001-11-23
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pubmed:abstractText |
Inherently unstable mammalian mRNAs contain AU-rich elements (AREs) within their 3' untranslated regions. Although found 15 years ago, the mechanism by which AREs dictate rapid mRNA decay is not clear. In yeast, 3'-to-5' mRNA degradation is mediated by the exosome, a multisubunit particle. We have purified and characterized the human exosome by mass spectrometry and found its composition to be similar to its yeast counterpart. Using a cell-free RNA decay system, we demonstrate that the mammalian exosome is required for rapid degradation of ARE-containing RNAs but not for poly(A) shortening. The mammalian exosome does not recognize ARE-containing RNAs on its own. ARE recognition requires certain ARE binding proteins that can interact with the exosome and recruit it to unstable RNAs, thereby promoting their rapid degradation.
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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/3' Untranslated Regions,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/KHSRP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thymine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/thymidine 5'-triphosphate
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
451-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11719186-3' Untranslated Regions,
pubmed-meshheading:11719186-Amino Acid Sequence,
pubmed-meshheading:11719186-Animals,
pubmed-meshheading:11719186-Base Pairing,
pubmed-meshheading:11719186-Base Sequence,
pubmed-meshheading:11719186-Cell-Free System,
pubmed-meshheading:11719186-Gene Silencing,
pubmed-meshheading:11719186-Genes, fos,
pubmed-meshheading:11719186-Humans,
pubmed-meshheading:11719186-Interleukin-2,
pubmed-meshheading:11719186-Jurkat Cells,
pubmed-meshheading:11719186-Mammals,
pubmed-meshheading:11719186-Molecular Sequence Data,
pubmed-meshheading:11719186-Poly A,
pubmed-meshheading:11719186-RNA, Messenger,
pubmed-meshheading:11719186-RNA, Neoplasm,
pubmed-meshheading:11719186-RNA-Binding Proteins,
pubmed-meshheading:11719186-Recombinant Fusion Proteins,
pubmed-meshheading:11719186-Sequence Alignment,
pubmed-meshheading:11719186-Sequence Homology, Amino Acid,
pubmed-meshheading:11719186-Thymine Nucleotides,
pubmed-meshheading:11719186-Trans-Activators
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pubmed:year |
2001
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pubmed:articleTitle |
AU binding proteins recruit the exosome to degrade ARE-containing mRNAs.
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pubmed:affiliation |
Department of Pharmacology, Laboratory of Gene Regulation and Signal Transduction, University of California, San Diego, La Jolla, CA 92093, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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