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Volumn 512, Issue , 2012, Pages 71-92

Methods applied to the study of protein arginine methylation

Author keywords

CARM1; Epigenetic; Histone methylation; PRMT1; PRMT5

Indexed keywords

5' METHYLTHIOADENOSINE PHOSPHORYLASE; 6 N,N' DIMETHYLARGININE; CELL EXTRACT; METHYLTRANSFERASE; METHYLTRANSFERASE INHIBITOR; N(G),N(G) DIMETHYLARGININE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEINASE INHIBITOR; RECOMBINANT ENZYME; S ADENOSYLMETHIONINE; SINEFUNGIN; TETRACYCLINE;

EID: 84865322765     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-391940-3.00004-4     Document Type: Chapter
Times cited : (26)

References (57)
  • 1
    • 0031025092 scopus 로고    scopus 로고
    • A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type i interferon receptor
    • C. Abramovich, B. Yakobson, J. Chebath, and M. Revel A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor The EMBO Journal 16 1997 260 266
    • (1997) The EMBO Journal , vol.16 , pp. 260-266
    • Abramovich, C.1    Yakobson, B.2    Chebath, J.3    Revel, M.4
  • 3
    • 23844534430 scopus 로고    scopus 로고
    • The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: Development of novel inhibitors
    • J.L. Anderson, B.S. Henriksen, R.A. Gibbs, and C.A. Hrycyna The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: Development of novel inhibitors The Journal of Biological Chemistry 280 2005 29454 29461
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 29454-29461
    • Anderson, J.L.1    Henriksen, B.S.2    Gibbs, R.A.3    Hrycyna, C.A.4
  • 4
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • M.T. Bedford, and S.G. Clarke Protein arginine methylation in mammals: Who, what, and why Molecular Cell 33 2009 1 13
    • (2009) Molecular Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 7
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein
    • H. Brahms, L. Meheus, V. de Brabandere, U. Fischer, and R. Luhrmann Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein RNA 7 2001 1531 1542
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 8
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • H. Brahms, J. Raymackers, A. Union, F. de Keyser, L. Meheus, and R. Luhrmann The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies The Journal of Biological Chemistry 275 2000 17122 17129
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3    De Keyser, F.4    Meheus, L.5    Luhrmann, R.6
  • 9
    • 1942534606 scopus 로고    scopus 로고
    • A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues
    • C.J. Brame, M.F. Moran, and L.D. McBroom-Cerajewski A mass spectrometry based method for distinguishing between symmetrically and asymmetrically dimethylated arginine residues Rapid Communications in Mass Spectrometry 18 2004 877 881
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , pp. 877-881
    • Brame, C.J.1    Moran, M.F.2    McBroom-Cerajewski, L.D.3
  • 10
    • 78751484386 scopus 로고    scopus 로고
    • Xenoestrogens regulate the activity of arginine methyltransferases
    • D. Cheng, and M.T. Bedford Xenoestrogens regulate the activity of arginine methyltransferases Chembiochem 12 2011 323 329
    • (2011) Chembiochem , vol.12 , pp. 323-329
    • Cheng, D.1    Bedford, M.T.2
  • 11
    • 33846001366 scopus 로고    scopus 로고
    • The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing
    • D. Cheng, J. Cote, S. Shaaban, and M.T. Bedford The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing Molecular Cell 25 2007 71 83
    • (2007) Molecular Cell , vol.25 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 15
    • 0021101952 scopus 로고
    • Methylation of elongation factor 1 alpha in mouse 3T3B and 3T3B/SV40 cells
    • N.J. Coppard, B.F. Clark, and F. Cramer Methylation of elongation factor 1 alpha in mouse 3T3B and 3T3B/SV40 cells FEBS Letters 164 1983 330 334
    • (1983) FEBS Letters , vol.164 , pp. 330-334
    • Coppard, N.J.1    Clark, B.F.2    Cramer, F.3
  • 17
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • J. Cote, and S. Richard Tudor domains bind symmetrical dimethylated arginines The Journal of Biological Chemistry 280 2005 28476 28483
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 19
    • 48749108946 scopus 로고    scopus 로고
    • Protein methyltransferase activities in commercial in vitro translation systems
    • R.B. Denman Protein methyltransferase activities in commercial in vitro translation systems Journal of Biochemistry 144 2008 223 233
    • (2008) Journal of Biochemistry , vol.144 , pp. 223-233
    • Denman, R.B.1
  • 20
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • A. Di Lorenzo, and M.T. Bedford Histone arginine methylation FEBS Letters 585 2011 2024 2031
    • (2011) FEBS Letters , vol.585 , pp. 2024-2031
    • Di Lorenzo, A.1    Bedford, M.T.2
  • 21
    • 0019794275 scopus 로고
    • Reversible methylation of cytoskeletal and membrane proteins in intact human erythrocytes
    • C. Freitag, and S. Clarke Reversible methylation of cytoskeletal and membrane proteins in intact human erythrocytes The Journal of Biological Chemistry 256 1981 6102 6108
    • (1981) The Journal of Biological Chemistry , vol.256 , pp. 6102-6108
    • Freitag, C.1    Clarke, S.2
  • 22
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • W.J. Friesen, S. Massenet, S. Paushkin, A. Wyce, and G. Dreyfuss SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets Molecular Cell 7 2001 1111 1117
    • (2001) Molecular Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1    Massenet, S.2    Paushkin, S.3    Wyce, A.4    Dreyfuss, G.5
  • 23
    • 79551606798 scopus 로고    scopus 로고
    • Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation
    • J.M. Hsu, C.T. Chen, C.K. Chou, H.P. Kuo, L.Y. Li, and C.Y. Lin Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation Nature Cell Biology 13 2011 174 181
    • (2011) Nature Cell Biology , vol.13 , pp. 174-181
    • Hsu, J.M.1    Chen, C.T.2    Chou, C.K.3    Kuo, H.P.4    Li, L.Y.5    Lin, C.Y.6
  • 24
    • 68949200962 scopus 로고    scopus 로고
    • Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody
    • C.J. Hung, Y.J. Lee, D.H. Chen, and C. Li Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody The Protein Journal 28 2009 139 147
    • (2009) The Protein Journal , vol.28 , pp. 139-147
    • Hung, C.J.1    Lee, Y.J.2    Chen, D.H.3    Li, C.4
  • 27
    • 0036205436 scopus 로고    scopus 로고
    • PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays
    • J. Lee, and M.T. Bedford PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays EMBO Reports 3 2002 268 273
    • (2002) EMBO Reports , vol.3 , pp. 268-273
    • Lee, J.1    Bedford, M.T.2
  • 29
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: Protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Y.H. Lee, and M.R. Stallcup Minireview: Protein arginine methylation of nonhistone proteins in transcriptional regulation Molecular Endocrinology 23 2009 425 433
    • (2009) Molecular Endocrinology , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 31
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • W.J. Lin, J.D. Gary, M.C. Yang, S. Clarke, and H.R. Herschman The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase The Journal of Biological Chemistry 271 1996 15034 15044
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 32
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Q. Liu, and G. Dreyfuss In vivo and in vitro arginine methylation of RNA-binding proteins Molecular and Cellular Biology 15 1995 2800 2808
    • (1995) Molecular and Cellular Biology , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 35
    • 17644382927 scopus 로고    scopus 로고
    • S-adenosyl-L-methionine: Transcellular transport and uptake by Caco-2 cells and hepatocytes
    • J.M. McMillan, U.K. Walle, and T. Walle S-adenosyl-L-methionine: Transcellular transport and uptake by Caco-2 cells and hepatocytes The Journal of Pharmacy and Pharmacology 57 2005 599 605
    • (2005) The Journal of Pharmacy and Pharmacology , vol.57 , pp. 599-605
    • McMillan, J.M.1    Walle, U.K.2    Walle, T.3
  • 36
    • 84856733701 scopus 로고    scopus 로고
    • Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance
    • V. Migliori, J. Muller, S. Phalke, D. Low, M. Bezzi, and W.C. Mok Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance Nature Structural & Molecular Biology 19 2012 136 144
    • (2012) Nature Structural & Molecular Biology , vol.19 , pp. 136-144
    • Migliori, V.1    Muller, J.2    Phalke, S.3    Low, D.4    Bezzi, M.5    Mok, W.C.6
  • 37
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • T.B. Miranda, M. Miranda, A. Frankel, and S. Clarke PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity The Journal of Biological Chemistry 279 2004 22902 22907
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 38
    • 33845789120 scopus 로고    scopus 로고
    • The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation
    • H. Naeem, D. Cheng, Q. Zhao, C. Underhill, M. Tini, and M.T. Bedford The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation Molecular and Cellular Biology 27 2007 120 134
    • (2007) Molecular and Cellular Biology , vol.27 , pp. 120-134
    • Naeem, H.1    Cheng, D.2    Zhao, Q.3    Underhill, C.4    Tini, M.5    Bedford, M.T.6
  • 39
    • 0041668113 scopus 로고    scopus 로고
    • Methods and tips for the purification of human histone methyltransferases
    • K. Nishioka, and D. Reinberg Methods and tips for the purification of human histone methyltransferases Methods 31 2003 49 58
    • (2003) Methods , vol.31 , pp. 49-58
    • Nishioka, K.1    Reinberg, D.2
  • 40
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • S.-E. Ong, G. Mittler, and M. Mann Identifying and quantifying in vivo methylation sites by heavy methyl SILAC Narure Methods 1 2004 119 126
    • (2004) Narure Methods , vol.1 , pp. 119-126
    • Ong, S.-E.1    Mittler, G.2    Mann, M.3
  • 41
    • 0014409081 scopus 로고
    • Protein methylase I. Purification and properties of the enzyme
    • W.K. Paik, and S. Kim Protein methylase I. Purification and properties of the enzyme The Journal of Biological Chemistry 243 1968 2108 2114
    • (1968) The Journal of Biological Chemistry , vol.243 , pp. 2108-2114
    • Paik, W.K.1    Kim, S.2
  • 43
    • 0035815625 scopus 로고    scopus 로고
    • Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
    • J. Rho, S. Choi, Y.R. Seong, W.K. Cho, S.H. Kim, and D.S. Im Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family The Journal of Biological Chemistry 276 2001 11393 11401
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 11393-11401
    • Rho, J.1    Choi, S.2    Seong, Y.R.3    Cho, W.K.4    Kim, S.H.5    Im, D.S.6
  • 46
    • 79251553753 scopus 로고    scopus 로고
    • The structural basis for tight control of PP2A methylation and function by LCMT-1
    • V. Stanevich, L. Jiang, K.A. Satyshur, Y. Li, P.D. Jeffrey, and Z. Li The structural basis for tight control of PP2A methylation and function by LCMT-1 Molecular Cell 41 2011 331 342
    • (2011) Molecular Cell , vol.41 , pp. 331-342
    • Stanevich, V.1    Jiang, L.2    Satyshur, K.A.3    Li, Y.4    Jeffrey, P.D.5    Li, Z.6
  • 48
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • S.D. Taverna, H. Li, A.J. Ruthenburg, C.D. Allis, and D.J. Patel How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers Nature Structural & Molecular Biology 14 2007 1025 1040
    • (2007) Nature Structural & Molecular Biology , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 50
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • M.L. Tradewell, Z. Yu, M. Tibshirani, M.C. Boulanger, H.D. Durham, and S. Richard Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations Human Molecular Genetics 21 2012 136 149
    • (2012) Human Molecular Genetics , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 52
    • 60649099160 scopus 로고    scopus 로고
    • Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry
    • H. Wang, R.M. Straubinger, J.M. Aletta, J. Cao, X. Duan, and H. Yu Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry Journal of the American Society for Mass Spectrometry 20 2009 507 519
    • (2009) Journal of the American Society for Mass Spectrometry , vol.20 , pp. 507-519
    • Wang, H.1    Straubinger, R.M.2    Aletta, J.M.3    Cao, J.4    Duan, X.5    Yu, H.6
  • 53
    • 82755176334 scopus 로고    scopus 로고
    • Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs
    • C. Wilczek, R. Chitta, E. Woo, J. Shabanowitz, B.T. Chait, and D.F. Hunt Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs The Journal of Biological Chemistry 286 2011 42221 42231
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 42221-42231
    • Wilczek, C.1    Chitta, R.2    Woo, E.3    Shabanowitz, J.4    Chait, B.T.5    Hunt, D.F.6
  • 55
    • 78650233514 scopus 로고    scopus 로고
    • TDRD3 is an effector molecule for arginine-methylated histone marks
    • Y. Yang, Y. Lu, A. Espejo, J. Wu, W. Xu, and S. Liang TDRD3 is an effector molecule for arginine-methylated histone marks Molecular Cell 40 2010 1016 1023
    • (2010) Molecular Cell , vol.40 , pp. 1016-1023
    • Yang, Y.1    Lu, Y.2    Espejo, A.3    Wu, J.4    Xu, W.5    Liang, S.6
  • 56
    • 66349133369 scopus 로고    scopus 로고
    • A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation
    • Z. Yu, T. Chen, J. Hebert, E. Li, and S. Richard A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation Molecular and Cellular Biology 29 2009 2982 2996
    • (2009) Molecular and Cellular Biology , vol.29 , pp. 2982-2996
    • Yu, Z.1    Chen, T.2    Hebert, J.3    Li, E.4    Richard, S.5
  • 57
    • 84858040000 scopus 로고    scopus 로고
    • Human protein arginine methyltransferase 7 (PRMT7) is a Type III enzyme forming omega-NG-monomethylated arginine residues
    • C.I. Zurita-Lopez, T. Sandberg, R. Kelly, and S.G. Clarke Human protein arginine methyltransferase 7 (PRMT7) is a Type III enzyme forming omega-NG-monomethylated arginine residues The Journal of Biological Chemistry 287 2012 7859 7870
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 7859-7870
    • Zurita-Lopez, C.I.1    Sandberg, T.2    Kelly, R.3    Clarke, S.G.4


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