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
Externally publishedYes

Fingerprint

Protein-Arginine N-Methyltransferases
Myelin Basic Protein
Histones
Brain
Pancreatic Ribonuclease
Peptide Fragments
Globulins
Methyltransferases
Substrates
Bovine Serum Albumin
Tryptophan
Methionine
Arginine
Proteins
Enzymes

Keywords

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

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Myelin basic protein inhibits histone-specific protein methylase I. / Park, Gil-Hong; Chanderkar, Latika P.; Paik, Woon Ki; Kim, Sangduk.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 874, No. 1, 07.11.1986, p. 30-36.

Research output: Contribution to journalArticle

Park, Gil-Hong ; Chanderkar, Latika P. ; Paik, Woon Ki ; Kim, Sangduk. / Myelin basic protein inhibits histone-specific protein methylase I. In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1986 ; Vol. 874, No. 1. pp. 30-36.
@article{1fc948725ff34f7fba63053cbc31bbf7,
title = "Myelin basic protein inhibits histone-specific protein methylase I",
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.",
keywords = "(Brain), Enzyme inhibitor, Histone-specific protein methylase I, Myelin basic protein, Protein-arginine-methyltransferase",
author = "Gil-Hong Park and Chanderkar, {Latika P.} and Paik, {Woon Ki} and Sangduk Kim",
year = "1986",
month = "11",
day = "7",
doi = "10.1016/0167-4838(86)90098-1",
language = "English",
volume = "874",
pages = "30--36",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "1",

}

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

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

UR - http://www.scopus.com/inward/citedby.url?scp=0022994934&partnerID=8YFLogxK

U2 - 10.1016/0167-4838(86)90098-1

DO - 10.1016/0167-4838(86)90098-1

M3 - Article

VL - 874

SP - 30

EP - 36

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 1

ER -