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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7083
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pubmed:dateCreated |
2006-3-23
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pubmed:abstractText |
A fundamental aspect of the biogenesis and function of eukaryotic messenger RNA is the quality control systems that recognize and degrade non-functional mRNAs. Eukaryotic mRNAs where translation termination occurs too soon (nonsense-mediated decay) or fails to occur (non-stop decay) are rapidly degraded. We show that yeast mRNAs with stalls in translation elongation are recognized and targeted for endonucleolytic cleavage, referred to as 'no-go decay'. The cleavage triggered by no-go decay is dependent on translation and involves Dom34p and Hbs1p. Dom34p and Hbs1p are similar to the translation termination factors eRF1 and eRF3 (refs 3, 4), indicating that these proteins might function in recognizing the stalled ribosome and triggering endonucleolytic cleavage. No-go decay provides a mechanism for clearing the cell of stalled translation elongation complexes, which could occur as a result of damaged mRNAs or ribosomes, or as a mechanism of post-transcriptional control.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-10508173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-10558994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-11027292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-11812856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-11909951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-11910110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-12105207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-12730326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-12853641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-12867083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-12869712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-12923185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-1394434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-14580341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-14744860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-14970383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-15040442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-15099522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-15175755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-15189161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-15965245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-16027170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-16554791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-2474074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-7891709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-8052314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-8393418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-9482746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16554824-9584085
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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/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dom34 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HBS1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1476-4687
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
440
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
561-4
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pubmed:dateRevised |
2011-1-5
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pubmed:meshHeading |
pubmed-meshheading:16554824-Cell Cycle Proteins,
pubmed-meshheading:16554824-Endoribonucleases,
pubmed-meshheading:16554824-GTP-Binding Proteins,
pubmed-meshheading:16554824-Genes, Reporter,
pubmed-meshheading:16554824-HSP70 Heat-Shock Proteins,
pubmed-meshheading:16554824-Peptide Chain Elongation, Translational,
pubmed-meshheading:16554824-Peptide Elongation Factors,
pubmed-meshheading:16554824-RNA, Fungal,
pubmed-meshheading:16554824-RNA, Messenger,
pubmed-meshheading:16554824-RNA Stability,
pubmed-meshheading:16554824-Ribosomes,
pubmed-meshheading:16554824-Saccharomyces cerevisiae,
pubmed-meshheading:16554824-Saccharomyces cerevisiae Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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