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rdf:type |
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lifeskim:mentions |
umls-concept:C0002345,
umls-concept:C0014241,
umls-concept:C0017337,
umls-concept:C0033268,
umls-concept:C0072388,
umls-concept:C0597298,
umls-concept:C0851285,
umls-concept:C1418833,
umls-concept:C1956003,
umls-concept:C1999216,
umls-concept:C2700640
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pubmed:issue |
1
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pubmed:dateCreated |
2000-1-11
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pubmed:abstractText |
ARD-1 is an endoribonuclease identified initially as the product of a human cDNA that complements mutations in rne, a gene that encodes Escherichia coli ribonuclease E. NIPP-1 was identified in bovine nuclear extracts as an inhibitor of protein phosphatase-1. Earlier work has shown that the protein-coding sequence of ARD-1 is identical to the carboxy-terminal third of NIPP-1. However, whether ARD-1 is present in eukaryotes as a distinct entity has been unclear, as neither ARD-1-specific transcripts nor ARD-1 protein were detected in mammalian cells in earlier studies. Here we show that ARD-1 exists in human cells as a discrete protein, and that the ARD-1 and NIPP-1 peptides are isoforms encoded by a single gene and the same alternatively spliced precursor RNA. A retained intron containing multiple translation stop codons that are configured to terminate translation and initiate nonsense-mediated decay, limits the production of cellular ARD-1 protein. Our results establish the process by which functionally disparate ARD-1 and NIPP-1 peptides are generated from the protein-coding sequence of the same gene in human cells.
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pubmed:grant |
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/PPP1R8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase inhibitor-1
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
240
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45-55
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10564811-Alternative Splicing,
pubmed-meshheading:10564811-Base Sequence,
pubmed-meshheading:10564811-Carrier Proteins,
pubmed-meshheading:10564811-Cell Extracts,
pubmed-meshheading:10564811-Cell Line,
pubmed-meshheading:10564811-Cell Line, Transformed,
pubmed-meshheading:10564811-DNA, Complementary,
pubmed-meshheading:10564811-Endoribonucleases,
pubmed-meshheading:10564811-Exons,
pubmed-meshheading:10564811-Gene Expression Regulation,
pubmed-meshheading:10564811-Genes,
pubmed-meshheading:10564811-Humans,
pubmed-meshheading:10564811-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10564811-Introns,
pubmed-meshheading:10564811-Molecular Sequence Data,
pubmed-meshheading:10564811-Phosphoprotein Phosphatases,
pubmed-meshheading:10564811-Protein Isoforms,
pubmed-meshheading:10564811-Protein Phosphatase 1,
pubmed-meshheading:10564811-RNA, Messenger,
pubmed-meshheading:10564811-RNA Precursors,
pubmed-meshheading:10564811-RNA-Binding Proteins,
pubmed-meshheading:10564811-Sequence Analysis, DNA,
pubmed-meshheading:10564811-Sequence Homology, Nucleic Acid,
pubmed-meshheading:10564811-Transcription, Genetic,
pubmed-meshheading:10564811-Tumor Cells, Cultured
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pubmed:year |
1999
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pubmed:articleTitle |
Alternative splicing regulates the production of ARD-1 endoribonuclease and NIPP-1, an inhibitor of protein phosphatase-1, as isoforms encoded by the same gene.
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pubmed:affiliation |
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee, UK.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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