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rdf:type |
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lifeskim:mentions |
umls-concept:C0005221,
umls-concept:C0035696,
umls-concept:C0043342,
umls-concept:C0086418,
umls-concept:C0205307,
umls-concept:C0243125,
umls-concept:C0699900,
umls-concept:C1148807,
umls-concept:C1257751,
umls-concept:C1421881,
umls-concept:C2348205
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pubmed:issue |
9
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pubmed:dateCreated |
2003-8-18
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pubmed:abstractText |
beta-globin mRNA bearing a nonsense codon is degraded in the cytoplasm of erythroid cells by endonuclease cleavage, preferentially at UG dinucleotides. An endonuclease activity in polysomes of MEL cells cleaved beta-globin and albumin mRNA in vitro at many of the same sites as PMR1, an mRNA endonuclease purified from Xenopus liver. Stable transfection of MEL cells expressing normal human beta-globin mRNA with a plasmid vector expressing the catalytically active form of PMR1 reduced the half-life of beta-globin mRNA from 12 to 1-2 h without altering GAPDH mRNA decay. The reduced stability of beta-globin mRNA in these cells was accompanied by an increase in the production of mRNA decay products corresponding to those seen in the degradation of nonsense-containing beta-globin mRNA. Therefore, beta-globin mRNA is cleaved in vivo by an endonuclease with properties similar to PMR1. Inhibiting translation with cycloheximide stabilized nonsense-containing beta-globin mRNA, resulting in a fivefold increase in its steady-state level. Taken together, our results indicate that the surveillance of nonsense-containing beta-globin mRNA in erythroid cells is a cytoplasmic process that functions on translating mRNA, and endonucleolytic cleavage constitutes one step in the process of beta-globin mRNA decay.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-10075884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-10622735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-10637233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-10884343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-10966469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11050168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11152474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11207359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11222765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11329012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11586900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11719186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-11782436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-12218187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-12242335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-12417715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-12457569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-12486012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-12769863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-1324170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-1545796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-1922078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-1931972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-2295312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-2325645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-2384211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-2573525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-6101206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-7890744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-7909515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-8114742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-9016622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-9049243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-9632780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-9737991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12923263-9848652
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1355-8382
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1157-67
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12923263-Animals,
pubmed-meshheading:12923263-Codon, Nonsense,
pubmed-meshheading:12923263-Cycloheximide,
pubmed-meshheading:12923263-Endoribonucleases,
pubmed-meshheading:12923263-Erythroid Precursor Cells,
pubmed-meshheading:12923263-Globins,
pubmed-meshheading:12923263-Humans,
pubmed-meshheading:12923263-Protein Synthesis Inhibitors,
pubmed-meshheading:12923263-RNA, Messenger,
pubmed-meshheading:12923263-Xenopus
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pubmed:year |
2003
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pubmed:articleTitle |
An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation of normal and nonsense-containing human beta-globin mRNA in erythroid cells.
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pubmed:affiliation |
Department of Molecular and Cellular Biochemistry and the Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio 43210, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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