Source:http://linkedlifedata.com/resource/pubmed/id/17049166
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2006-11-7
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pubmed:abstractText |
By selection of genetic suppressor elements (GSEs) conferring resistance to topoisomerase II inhibitors in Chinese hamster cells (DC-3F), we identified a gene encoding two proteins of 78 and 82 kDa which belong to the protein arginine methyltransferase (PRMT) family. Down-regulation of these enzymes (named PRMT7alpha and beta), either induced by an antisense GSE or as observed in the 9-OH-ellipticine (9-OH-E) resistant mutant DC-3F/9-OH-E, was responsible for cell resistance to various DNA damaging agents. Alternative splicing alterations in the 5'-terminal region and changes of the polyadenylation site of PRMT7 mRNAs were observed in these resistant mutant cells. PRMT7alpha and beta are isoforms of a highly conserved protein containing two copies of a module common to all PRMTs, comprising a Rossmann-fold domain and a beta-barrel domain. The C-terminal repeat appears to be degenerate and catalytically inactive. PRMT7alpha and beta form homo- and hetero-dimers but differ by their sub-cellular localization and in vitro recognize different substrates. PRMT7beta was only observed in Chinese hamster cells while mouse 10T1/2 fibroblasts only contain PRMT7alpha. Surprisingly, in human cells the anti-PRMT7 antibody essentially recognized an approximately 37 kDa peptide, which is not formed during extraction, and a faint band at 78 kDa. Analysis of in vitro and in vivo methylation patterns in cell lines under- or over-expressing PRMT7alpha and beta detected a discrete number of proteins which methylation and/or expression are under the control of these enzymes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Topoisomerases, Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/PRMT7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Arginine...,
http://linkedlifedata.com/resource/pubmed/chemical/Topoisomerase II Inhibitors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1760
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1646-56
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:17049166-Animals,
pubmed-meshheading:17049166-Cell Cycle,
pubmed-meshheading:17049166-Cricetinae,
pubmed-meshheading:17049166-Cricetulus,
pubmed-meshheading:17049166-DNA Topoisomerases, Type II,
pubmed-meshheading:17049166-Dimerization,
pubmed-meshheading:17049166-Enzyme Inhibitors,
pubmed-meshheading:17049166-HeLa Cells,
pubmed-meshheading:17049166-Humans,
pubmed-meshheading:17049166-Isoenzymes,
pubmed-meshheading:17049166-Methylation,
pubmed-meshheading:17049166-Methyltransferases,
pubmed-meshheading:17049166-Mice,
pubmed-meshheading:17049166-Protein-Arginine N-Methyltransferases,
pubmed-meshheading:17049166-Species Specificity,
pubmed-meshheading:17049166-Topoisomerase II Inhibitors,
pubmed-meshheading:17049166-Tumor Cells, Cultured
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pubmed:year |
2006
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pubmed:articleTitle |
Characterization of prmt7alpha and beta isozymes from Chinese hamster cells sensitive and resistant to topoisomerase II inhibitors.
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pubmed:affiliation |
CNRS FRE2618, Laboratoire de Pharmacologie des Agents Anticancéreux, Institut Bergonié, 229 Cours de l'Argonne, 33076 Bordeaux, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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