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Enzymatic Methylation of Arginine Residue in Myelin Basic Protein

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Advances in Post-Translational Modifications of Proteins and Aging

Part of the book series: Advances in Experimental Medicine and Biology ((NATO ASI F,volume 231))

Abstract

Post-translational methylation of protein is a multisite reaction occurring in several amino acid side chains of specific methyl acceptor proteins, utilizing S-adenosyl-L-methionine (AdoMet)* as the methyl donor (1,2). The major sites of the reaction have been identified as the nitrogen, oxygen and sulfur atoms, all nucleophilic in nature. Several review articles on protein methylation have appeared recently (3–5) and in the preceeding chapter of this book (6). This article is focused mainly on the relationship between protein-arginine methylation and the myelin basic protein (MBP).

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Abbreviations

AdoMet:

S-adenosyl-L-methionine

MBP:

myelin basic protein

MMA:

NG-monomethylarginine

sym-DMA:

NG, N’G-dimethylarginine

asym-DMA:

N2, N2-dimethylarginine

SCD:

subacute combined degeneration

References

  1. S. Kim, and W. K. Paik, Studies on the origin of ε-N-methyl-L-lysine in protein, J. Biol. Chem., 240:4629 (1965).

    PubMed  CAS  Google Scholar 

  2. W. K. Paik and S. Kim, Protein methylation, Science, 174:114 (1971).

    Article  PubMed  CAS  Google Scholar 

  3. W. K. Paik and S. Kim, Protein methylation, in: “Biochemistry: A Series of Monographs,” A Meister, ed., John Wiley & Sons, New York, 1:1 (1980).

    Google Scholar 

  4. W. K. Paik and S. Kim, Methylation and demethylation of protein, in: “The Enzymology of Post-Translation Modification of Proteins,” R. B. Freedman and H. C. Hawkins, eds., Academic Press, London, 2:187 (1985).

    Google Scholar 

  5. S. Clarke, Protein carboxyl methyltransferases: Two distinct classes of enzymes, Ann. Rev. Biochem., 54:479 (1985).

    Article  PubMed  CAS  Google Scholar 

  6. W. K. Paik, K. S. Park, B. F. Frost, and S. Kim, Effect of enzymatic methylation on the import of in vitro synthesized apocytochrome c into mitochondria, in: “Post-Translation Modifications of Proteins and Ageing,” Plenum Publishing Co., London, in this book (1987).

    Google Scholar 

  7. W. K. Paik and S. Kim, Protein methylase I, J. Biol. Chem., 243:2108 (1968).

    PubMed  CAS  Google Scholar 

  8. G. S. Baldwin and P. R. Carnegie, Specific enzymatic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin, Science, 171:579 (1971).

    Article  PubMed  CAS  Google Scholar 

  9. S. Brostoff and E. H. Eylar, Localization of methylated arginine in the Al protein from myelin, Proc. Natl. Acad. Sci. USA, 68:765 (1971).

    Article  PubMed  CAS  Google Scholar 

  10. W. H. Lee, S. Kim, and W. K. Paik, S-Adenosylmethionine:proteinarginine methyltransferase: Purification and mechanism of the enzyme, Biochemistry, 16:78 (1977).

    Article  PubMed  CAS  Google Scholar 

  11. E. H. Eylar, The structure and immunologic properties of myelin, Ann. N.Y. Acad. Sci., 195:481 (1972).

    Article  PubMed  CAS  Google Scholar 

  12. E. H. Eylar, Amino acid sequence of the basic protein of the myelin membrane, Proc. Natl. Acad. Sci. USA, 67:1425 (1970).

    Article  PubMed  CAS  Google Scholar 

  13. P. R. Carnegie, Amino acid sequence of the encephalitogenic basic protein from human myelin, Biochem. J., 123:57 (1971).

    PubMed  CAS  Google Scholar 

  14. P. R. Caregie, Properties, structure and possible neuroreceptor role of the encephalitogenic protein of human brain, Nature, 229:25 (1971).

    Article  Google Scholar 

  15. G. E. Deibler and R. E. Martenson, Determination of methylated basic amino acids with the amino acid analyzer, J. Biol. Chem., 248:2387 (1973).

    PubMed  CAS  Google Scholar 

  16. M. Reporter and J. L. Corbin, NG-NG-Dimethylarginine in myosin during muscle development, Biochem. Biophys. Res. Comm., 43:644 (1971).

    Article  CAS  Google Scholar 

  17. J. Karn, G. Vidali, L. C. Boffa, and V. G. Allfrey, Characterization of the non-histone nuclear proteins associated with rapidly labeled heterogeneous nuclear RNA, J. Biol. Chem., 252:7307 (1977).

    PubMed  CAS  Google Scholar 

  18. P. R. Dunkley and P. R. Carnegie, Amino acid sequence of the smaller basic protein from rat brain myelin, Biochem. J141:243 (1984).

    Google Scholar 

  19. W. Jacobson, G. Gandy and R. L. Sidman, Experimental subacute combined degeneration of the cord in mice, J. Pathol., 109:333 (1973).

    Google Scholar 

  20. J. J. Dinn, D. G. Weir, S. McCann, B. Reed, P. Wilson, and J. M. Scott, Methyl group deficiency in nerve tissue: A hypothesis to explain the lesion of subacute combined degeneration, Irish J. Med. Sci., 149:1 (1980).

    Google Scholar 

  21. J. M. Scott, J. J. Dinn, P. Wilson and D. G. Weir, Pathogenesis of subacute combined degeneration: A result of methyl group deficiency, The Lancet, 2:334 (1981).

    Article  CAS  Google Scholar 

  22. G. Gandy, W. Jacobson and R. Sidman, Inhibition of a transmethylation reaction in the central nervous system — A experimental model for subacute combined degeneration of the cord, J. Physiol., 233:1 (1973).

    Google Scholar 

  23. W. Jacobson and G. Gandy, Tunbridge Wells, An induced neurological disease in mice — Possibly a model for subacute combined degeneration of the cord, in: “Progress in Neurological Research,” P. O. Behan and F. C. Rose eds., Pitman Medical, England, 211 (1979).

    Google Scholar 

  24. J. B. Lombardini, A. W. Coulter, and P. Talalay, Analogues of methionine as substrates and inhibitors of the methionine ade-nosyltransferase reaction: Deductions concerning the conformation of methionine, Mol. Pharmacol., 6:481 (1970).

    PubMed  CAS  Google Scholar 

  25. A. J. Crang and W. Jacobson, The methylation in vitro of myelin basic protein by arginine methylase from mouse spinal cord, Biochem. Soc. Trans., 8:26 (1980).

    Google Scholar 

  26. D. H. Small, P. R. Carnegie, and R. Anderson, Cycloleucine-induced vacuolation of myelin is associated with inhibition of protein methylation, Neuroscience Lett., 21:287 (1981).

    Article  CAS  Google Scholar 

  27. A. J. Crang and W. Jacobson, The relationship of myelin basic protein (arginine) methyltransferase to myelination in mouse spinal cord, J. Neurochem., 39:244 (1982).

    Article  PubMed  CAS  Google Scholar 

  28. M. Miyake, and Y. Kakimoto, Protein methylation by cerebral tissue, J. Neurochem., 20: 859 (1973).

    Article  PubMed  CAS  Google Scholar 

  29. G.-H. Park, L. P. Chanderkar, W. K. Paik, and S. Kim, Myelin basic protein inhibits histone-specific protein methylase I Biochem. Biophys. Acta, 874:30 (1986).

    Article  CAS  Google Scholar 

  30. K. S. Park, S. Y. Hong, H. W. Lee, S. Kim, and W. K. Paik, HPLC analysis of methylated amino acids: Methylated amino acids on HPLC, Arch. Biochem. Res., 9:15 (1986).

    CAS  Google Scholar 

  31. P. Morell, S. Greenfield, E. Constantino-Ceccarini, and H. Wisniewski, Changes in the protein composition of mouse brain myelin during development, J. Neurochem., 19:2545 (1972).

    Article  PubMed  CAS  Google Scholar 

  32. E. Barbarese, J. H. Carson, and P. E. Braun, Accumulation of the four myelin basic proteins in mouse brain during development, J. Neurochem., 31:779 (1978).

    Article  PubMed  CAS  Google Scholar 

  33. C. W. Campagnoni, G. D. Cary, and A. T. Campagnoni, Synthesis of myelin basic protein in the developing mouse brain, Arch. Biochem. Biophys., 190:118 (1978).

    Article  PubMed  CAS  Google Scholar 

  34. L. P. Chanderkar, W. K. Paik, and S. Kim, Studies on myelin basic protein methylation during mouse brain development, Biochem. J., 240:471 (1986).

    PubMed  CAS  Google Scholar 

  35. C. H. J. Chou, R. Shapira, and R. B. Friz, Encephalitogenic activity of the small form of mouse myelin basic protein in the SjL/J mouse, J. Immunol. 130:2183 (1983).

    PubMed  CAS  Google Scholar 

  36. N. Sundarraj and S. E. Pfeiffer, Myelin basic protein arginine methyl transferase: Wide distribution among both neurogenic and non-neurogenic tissues, Biochem. Biophys. Res. Commun., 52:1039 (1973).

    Article  PubMed  CAS  Google Scholar 

  37. W. K. Paik and S. Kim, Protein methylases during the development of rat brain, Biochem. Biophys. Acta, 313:181 (1973).

    Article  CAS  Google Scholar 

  38. G. M. Jones and P. R. Carnegie, Methylation of myelin basic protein by enzymes from rat brain, J. Neurochem. 23:1231 (1974).

    Article  PubMed  CAS  Google Scholar 

  39. J. L. Guenet, Mutants of the mouse with an abnormal myelination: A review for geneticists, in: “Neurological Mutations Affecting Myelination,” N. Baumann, ed., Elsevier/North-Holland, New York (1980).

    Google Scholar 

  40. S. Kim, M. Tuck, M. Kim, A. T. Champagnoni, and W. K. Paik, Studies on myelin basic protein-specific protein methylase I in various dysmyelinating mutant mice, Biochem. Biophys. Res. Commun., 123:468 (1984).

    Article  PubMed  CAS  Google Scholar 

  41. A. T. Campagnoni, C. W. Campagnoni, J.-M Bourre, C. Jacque, and N. Baumann, Cell-free synthesis of myelin basic proteins in normal and dysmyelinating mice, J. Neurochem., 42:733 (1984).

    Article  PubMed  CAS  Google Scholar 

  42. E. H. Eylar and M. Thompson, Allergic encephalomyelitis: The physico-chemical properties of the basic protein encephalitogen from bovine spinal cord, Arch. Biochem. Biophys., 129:468 (1969).

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Fels Research Institute, Temple University School of Medicine, Philadelphia, PA, 19140, USA

    Sangduk Kim, Latika P. Chanderkar, Subrata K. Ghosh, Jong-Ok Park & Woon Ki Paik

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  3. Subrata K. Ghosh
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  4. Jong-Ok Park
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Editors and Affiliations

  1. University of Naples, Naples, Italy

    Vincenzo Zappia , Patrizia Galletti  & Raffaele Porta ,  & 

  2. University of Texas Health Science Center, Houston, Texas, USA

    Finn Wold

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Kim, S., Chanderkar, L.P., Ghosh, S.K., Park, JO., Paik, W.K. (1988). Enzymatic Methylation of Arginine Residue in Myelin Basic Protein. In: Zappia, V., Galletti, P., Porta, R., Wold, F. (eds) Advances in Post-Translational Modifications of Proteins and Aging. Advances in Experimental Medicine and Biology, vol 231. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9042-8_26

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  • DOI: https://doi.org/10.1007/978-1-4684-9042-8_26

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-9044-2

  • Online ISBN: 978-1-4684-9042-8

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