Generation of polyclonal antiserum for the detection of methylarginine proteins

Journal of Immunological Methods

Volumn 320, Issue 1-2, 2007, Pages 132-142

  Duan, Peng ^a   Xu, Ye ^a   Birkaya, Barbara ^a   Myers, Jason ^a   Pelletier, Michel ^a   Read, Laurie K ^a   Guarnaccia, Corrado ^b   Pongor, Sandor ^b   Denman, Robert B ^c   Aletta, John M ^a  

^a UNIVERSITY AT BUFFALO   (United States)

^b INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^c NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

Asymmetrical dimethylarginine; FMRP; Nucleolin; Peptide synthesis

Indexed keywords

ARGININE; ARGININE METHYLTRANSFERASE 1; CELL EXTRACT; CELL PROTEIN; FRAGILE X MENTAL RETARDATION PROTEIN; GLYCINE; METHYLTRANSFERASE; NUCLEOLIN; POLYCLONAL ANTISERUM; RIBONUCLEIC ACID BINDING PROTEIN 16; RIBONUCLEOPROTEIN ANTIBODY; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL CULTURE; CELL STRAIN; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; MOLECULAR BIOLOGY; NONHUMAN; NUCLEOLUS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN LOCALIZATION; PROTEIN METHYLATION; PROTEIN MOTIF; PROTEIN SYNTHESIS; RAT; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ANTIBODY SPECIFICITY; ARGININE; FRAGILE X MENTAL RETARDATION PROTEIN; METHYLATION; MOLECULAR SEQUENCE DATA; NERVE GROWTH FACTORS; PC12 CELLS; PEPTIDES; PROTEINS; RATS;

EID: 33847377144     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2007.01.006     Document Type: Article

References (40)

1. Bakker W.J., Blazquez-Domingo M., Kolbus A., Besooyen J., Steinlein P., Beug H., Coffer P.J., Lowenberg B., von Lindern M., and van Dijk T.B. FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyltransferase 1. J. Cell Biol. 164 (2004) 175
2. Bedford M.T., and Richard S. Arginine methylation an emerging regulator of protein function. Mol. Cell 18 (2005) 263
3. Belyanskaya L.L., Gehrig P.M., and Gehring H. Exposure on cell surface and extensive arginine methylation of ewing sarcoma (EWS) protein. J. Biol. Chem. 276 (2001) 18681
4. Birkaya B., and Aletta J.M. NGF promotes copper accumulation required for optimum neurite outgrowth and protein methylation. J. Neurobiol. 63 (2005) 49
5. Boisvert F.M., Cote J., Boulanger M.C., Cleroux P., Bachand F., Autexier C., and Richard S. Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing. J. Cell Biol. 159 (2002) 957
6. Boisvert F.M., Cote J., Boulanger M.C., and Richard S. A proteomic analysis of arginine-methylated protein complexes. Mol. Cell. Proteomics 2 (2003) 1319
7. Cimato T.R., Ettinger M.J., Zhou X., and Aletta J.M. Nerve growth factor-specific regulation of protein methylation during neuronal differentiation of PC12 cells. J. Cell Biol. 138 (1997) 1089
8. Cimato T.R., Tang J., Xu Y., Guarnaccia C., Herschman H.R., Pongor S., and Aletta J.M. Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1 (PRMT1). J. Neurosci. Res. 67 (2002) 435
9. Cote J., Boisvert F.M., Boulanger M.C., Bedford M.T., and Richard S. Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. Mol. Biol. Cell 14 (2003) 274
10. Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H., Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P., Bannister A.J., and Kouzarides T. Histone deimination antagonizes arginine methylation. Cell 118 (2004) 545
11. Dolzhanskaya N., Merz G., Aletta J.M., and Denman R.B. Methylation regulates FMRP's intracellular protein-protein and protein-RNA interactions. J. Cell Sci. 119 (2006) 1933
12. Fields C.G., Lloyd D.H., Macdonald R.L., Otteson K.M., and Noble R.L. HBTU activation for automated Fmoc solid-phase peptide synthesis. Pept. Res. 4 (1991) 95
13. Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., and Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277 (2002) 3537
14. Friesen W.J., Massenet S., Paushkin S., Wyce A., and Dreyfuss G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell 7 (2001) 1111
15. Gary J.D., and Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic. Acid. Res. Mol. Biol. 61 (1998) 65
16. Glenney J.R., Zokas L., and Kamps M.P. Monoclonal antibodies to phosphotyrosine. J. Immunol. Methods 109 (1988) 277
17. Goulah C.C., Pelletier M., and Read L.K. Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins. RNA 12 (2006) 1545
18. Hayman M.L., and Read L.K. Trypanosoma brucei RBP16 is a mitochondrial Y-box family protein with guide RNA binding activity. J. Biol. Chem. 274 (1999) 12067
19. Hebert M.D., Shpargel K.B., Ospina J.K., Tucker K.E., and Matera G. Coilin methylation regulates nuclear body formation. Dev. Cell 3 (2002) 329
20. Lapeyre B., Amalric F., Ghaffari S.H., Rao S.V., Dumbar T.S., and Olson M. Protein and cDNA sequence of a glycine-rich, dimethylarginine-containing region located near the carboxyl-terminal end of nucleolin (C23 and 100 kDa). J. Biol. Chem. 261 (1986) 9167
21. Lee J., Sayegh J., Daniel J., Clarke S., and Bedford M.T. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J. Biol. Chem. 280 (2005) 32890
22. Lefebvre S., Burglen L., Reboullet S., Clermont O., Violet L., Benichou B., Cruaud C., Millaseau P., Zeviani M., et al. Identification and characterization of a spinal muscular atrophy-determining gene. Cell 80 (1995) 155
23. Lischwe M.A., Roberts K.D., Yeoman L.C., and Busch H. Nucleolar specific acidic phosphoprotein C23 is highly methylated. J. Biol. Chem. 257 (1982) 14600
24. Liu Q., and Dreyfuss G. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell. Biol. 15 (1995) 2800
25. Miranda T.B., Miranda M., Frankel A., and Clarke S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 279 (2004) 22902
26. Mobley W.C., Schenker A., and Shooter E.M. Characterization and isolation of proteolytically modified nerve growth factor. Biochemistry 15 (1976) 5543
27. Mowen K.A., Schurter B.T., Fathman J.W., David M., and Glimcher L.H. Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes. Mol. Cell 15 (2004) 559
28. Ong S.E., Mittler G., and Mann M. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 1 (2004) 119
29. Pelletier M., Xu Y., Wang X., Zahariev S., Pongor S., Aletta J.M., and Read L.K. Arginine methylation of a mitochondrial guide RNA binding protein from Trypanosoma brucei. Mol. Biochem. Parasitol. 118 (2001) 49
30. Rajpurohit R., Lee S.O., Park J.O., Paik W.K., and Kim S. Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase. J. Biol. Chem. 269 (1994) 1075
31. Rawal N., Rajpurohit R., Lischwe M.E., Williams K.R., Paik W.K., and Kim S. Structural specificity for S-adenosylmethionine:protein arginine N-methyltransferases. Biochim. Biophys. Acta 1248 (1995) 11
32. Rivier J., McClintock R., Galyean R., and Anderson H. Reversed-phase high-performance liquid chromatography: preparative purification of synthetic peptides. J. Chromatogr. 288 (1984) 303
33. Smith J.J., Rucknagel K.P., Schierhorn A., Tang J., Nemeth A., Linder M., Herschman H.R., and Wahle E. Unusual sites of arginine methylation in poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J. Biol. Chem. 274 (1999) 13229
34. Sparrow J.T., and Monera O.D. Improvements to the TMSBr method of peptide resin deprotection and cleavage: application to large peptides. Pept. Res. 9 (1996) 218
35. Stetler A., Winograd C., Sayegh J., Cheever A., Patton E., Zhang X., Clarke S., and Ceman S. Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp. Hum. Mol. Genet. 15 (2006) 87
36. Sung Y.J., Dolzhanskaya N., Nolin S.L., Brown T., Currie J.R., and Denman R.B. The fragile X mental retardation protein FMRP binds elongation factor 1A mRNA and negatively regulates its translation in vivo. J. Biol. Chem. 278 (2003) 15669
37. Székely Z., Zakhariev S., Guarnaccia C., Antcheva N., and Pongor S. A highly effective method for synthesis of Nw-substituted arginines as building blocks for Boc/Fmoc peptide chemistry. Tetr. Lett. 40 (1999) 4439
38. Wada K., Inoue K., and Hagiwara M. Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy. Biochim. Biophys. Acta 1591 (2002) 1
39. Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L., Sonbuchner S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G., Clarke S., Stallcup M.R., Allis C.D., and Coonrod S.A. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 306 (2004) 279
40. Xu W., Chen H., Du K., Aashara H., Tini M., Emerson B.M., Montminy M., and Evans R.M. A transcriptional switch mediated by cofactor methylation. Science 294 (2001) 2507