Myelin basic protein inhibits histone-specific protein methylase I

Gil Hong Park, Latika P. Chanderkar, Woon Ki Paik, Sangduk Kim

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Bovine brain myelin basic protein, free of associated proteolytic activity, was found to be a specific inhibitor of histone-specific protein methylase I (S-adenosyl-l-methionine:protein-l-arginine N-methyltransferase, EC 2.1.1.23) purified from bovine brain. 50% of the methyl group incorporation into the histone substrate catalyzed by the methylase I was inhibited by myelin basic protein at a concentration of 0.326 mM. However, neither of the peptide fragments (residues 1-116 and residues 117-170) generated by the chemical cleavage of myelin basic protein at the tryptophan residue retained the inhibitory activity for histone-specific protein methylase I. Proteins such as γ-globulin, bovine serum albumin, bovine pancreatic ribonuclease and polyarginine did not exhibit significant inhibitory activity toward the enzyme. The Ki value for myelin basic protein was estimated to be 3.42 · 10-5 M for histone-specific protein methylase I and the nature of the inhibition was uncompetitive toward histone substrate.

Original languageEnglish
Pages (from-to)30-36
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume874
Issue number1
DOIs
Publication statusPublished - 1986 Nov 7

Keywords

  • (Brain)
  • Enzyme inhibitor
  • Histone-specific protein methylase I
  • Myelin basic protein
  • Protein-arginine-methyltransferase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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