Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin

Science. 1971 Feb 12;171(3971):579-81. doi: 10.1126/science.171.3971.579.

Abstract

A cytoplasmic enzyme from guinea pig brain was shown to transfer methyl groups from S-adenosylmethionine to only one of 19 arginine residues in the basic protein from human brain. The products were omega-N-monomethylarginine and omega-N,N'-dimethylarginine. These methylated arginines are adjacent to the main encephalitogenic determinant in the protein. Methylation may aid in the transfer of this region of the protein into the nonpolar environment within myelin and in maintaining the integrity of myelin.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine / metabolism*
  • Autoradiography
  • Brain / enzymology
  • Carbon Isotopes
  • Demyelinating Diseases / etiology
  • Encephalomyelitis, Autoimmune, Experimental / metabolism*
  • Guinea Pigs
  • Humans
  • Methionine / metabolism
  • Methylation*
  • Myelin Sheath / metabolism*
  • Nerve Tissue Proteins / analysis
  • Nerve Tissue Proteins / metabolism*
  • Nucleosides / metabolism
  • Pepsin A
  • Peptides / analysis
  • Transferases / metabolism
  • Trypsin
  • Vitamin B 12 Deficiency / complications

Substances

  • Carbon Isotopes
  • Nerve Tissue Proteins
  • Nucleosides
  • Peptides
  • Arginine
  • Methionine
  • Transferases
  • Trypsin
  • Pepsin A