TY - JOUR
T1 - Myelin basic protein inhibits histone-specific protein methylase I
AU - Park, Gil Hong
AU - Chanderkar, Latika P.
AU - Paik, Woon Ki
AU - Kim, Sangduk
N1 - Funding Information:
This work was supported in part by Grant RG1765-A-1 from the National Multiple Sclerosis Society, BRSG 507 PRO5417 from National Institute of Health, CA 12227 from the National Cancer Institute, and AM09602 from the National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases.
PY - 1986/11/7
Y1 - 1986/11/7
N2 - 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.
AB - 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.
KW - (Brain)
KW - Enzyme inhibitor
KW - Histone-specific protein methylase I
KW - Myelin basic protein
KW - Protein-arginine-methyltransferase
UR - http://www.scopus.com/inward/record.url?scp=0022994934&partnerID=8YFLogxK
U2 - 10.1016/0167-4838(86)90098-1
DO - 10.1016/0167-4838(86)90098-1
M3 - Article
C2 - 2429705
AN - SCOPUS:0022994934
SN - 1570-9639
VL - 874
SP - 30
EP - 36
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 1
ER -