Literature DB >> 12517794

Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents.

Laurent Gros1, Charlotte Delaporte, Stéphane Frey, Julien Decesse, Bruno Robert de Saint-Vincent, Laurent Cavarec, Anne Dubart, Andrei V Gudkov, Alain Jacquemin-Sablon.   

Abstract

Genetic suppressor elements (GSEs) are cDNA fragments encoding either truncated proteins, acting as dominant-negative mutants, or inhibitory antisense RNA segments counteracting with the gene from which they are derived. To identify genes controlling the cell response to cytotoxic agents, a normalized retroviral library of randomly fragmented cDNAs from Chinese hamster cell line DC-3F was screened for GSEs conferring resistance to the topoisomerase II inhibitor 9-OH-ellipticine. From 218 cDNA fragments isolated, 11 functional GSEs, corresponding to at least 8 independent genes, were selected. The gene corresponding to the most abundant GSE encodes two proteins, p77 and p82, highly homologous to proteins detected in various species and carrying the sequence motifs characteristic of the protein arginine N-methyltransferase family. Furthermore, a methylase activity was observed on myelin basic protein in immunoprecipitates of hemagglutinin-tagged p77 and p82. Therefore, p77 and p82 are the first identified members of a new protein arginine N-methyltransferase family. A decreased expression of these enzymes is associated with either resistance or hypersensitivity to a broad range of DNA-damaging agents. Our data indicate that down-regulation of these enzymes in the GSE-expressing cells would alter one or several steps downstream of the drug-target interaction in the drug-response pathway.

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Year:  2003        PMID: 12517794

Source DB:  PubMed          Journal:  Cancer Res        ISSN: 0008-5472            Impact factor:   12.701


  24 in total

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2.  Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1.

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Review 3.  Histone arginine methylation.

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4.  Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis.

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Journal:  Mol Cell Biol       Date:  2006-05       Impact factor: 4.272

Review 5.  PRMT7 as a unique member of the protein arginine methyltransferase family: A review.

Authors:  Kanishk Jain; Steven G Clarke
Journal:  Arch Biochem Biophys       Date:  2019-02-22       Impact factor: 4.013

6.  Methylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expression.

Authors:  Marie-Chloé Boulanger; Chen Liang; Rodney S Russell; Rongtuan Lin; Mark T Bedford; Mark A Wainberg; Stéphane Richard
Journal:  J Virol       Date:  2005-01       Impact factor: 5.103

Review 7.  Role of PRMTs in cancer: Could minor isoforms be leaving a mark?

Authors:  R Mitchell Baldwin; Alan Morettin; Jocelyn Côté
Journal:  World J Biol Chem       Date:  2014-05-26

8.  Cloning, expression, purification and preliminary X-ray crystallographic analysis of mouse protein arginine methyltransferase 7.

Authors:  Vincent Cura; Nathalie Troffer-Charlier; Marie-Annick Lambert; Luc Bonnefond; Jean Cavarelli
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2013-12-24       Impact factor: 1.056

9.  Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.

Authors:  Cecilia I Zurita-Lopez; Troy Sandberg; Ryan Kelly; Steven G Clarke
Journal:  J Biol Chem       Date:  2012-01-12       Impact factor: 5.157

10.  A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation.

Authors:  Zhenbao Yu; Taiping Chen; Josée Hébert; En Li; Stéphane Richard
Journal:  Mol Cell Biol       Date:  2009-03-16       Impact factor: 4.272

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