Myelin basic protein inhibits histone-specific protein methylase I

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

doi:10.1016/0167-4838(86)90098-1

Cited by 13 publications

(2 citation statements)

References 27 publications

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“…On the other hand, inhibitors that act on methyl-acceptor subsrate site has not been well studied, except that myelin basic protein (MBP) which has been shown to inhibit histone-specific PM I from calf brain (Park et al, 1986). This basic protein is the only known methyl acceptor for MBP-specific PM I: It is noted that molecular and catalytic properties of these two subclasses of PM I's are quite different from each other (Ghosh et al, 1988;Rajpurohit et al, 1994).…”

Section: Discussionmentioning

confidence: 98%

Inhibitory effect of arginine-derivatives from ginseng extract and basic amino acids on protein-arginine N-methyltransferase

et al. 1999

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Protein-arginine N-methyltransferase (protein methylase I) catalyzes methylation of arginyl residues on substrate protein posttranslationally utilizing S-adenosyl-L-methionine as the methyl donor and yields NG-methylarginine residues. Arginyl-fructose and arginyl-fructosyl-glucose from Korean red ginseng were found to inhibit protein methylase I activity in vitro. This inhibitory activity was shown to be due to arginyl moiety in the molecules, rather than that of carbohydrates. Several basic amino acids as well as polyamines were also found to inhibit protein methylase I activity. Interestingly, the intensity of the inhibitory activity was correlated with the number of amino-group in polyamines, thus, in the order of spermine > spermidine > putrescine > agmatine-sulfate, with IC50 at approximately 15 mM, 25 mM, 35 mM, and 50 mM, respectively. On the other hand, neutral amino acids or NaCl did not inhibit the enzyme activity. Lineweaver-Burk plot analysis of the protein methylase I activity in the presence of arginine and spermidine indicated that the inhibition was competitive in nature in respect to protein substrate, with the Ki values of 24.8 mM and 11.5 mM, respectively.

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Section: Discussionmentioning

confidence: 98%

Inhibitory effect of arginine-derivatives from ginseng extract and basic amino acids on protein-arginine N-methyltransferase

et al. 1999

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“…Sensitivities toward p-chloromercuribenzoate and guanidine-HC1 as well as heat inactivation profiles also differ markedly among the enzymes. Interestingly, MBP, a high affinity substrate for MBP-specific protein methylase I, acted as an inhibitor for the nuclear protein/histone-specific enzyme with K i value of 3.42 × 10 6M (Park et al, 1986). Related to this, our recent study showed that several basic amino acids such as arginine, lysine and histidine, as well as polyamines were found to inhibit the rat liver protein methylase I at relatively high concentrations (Yoo et al, 1998).…”

Section: A Mammalian Organsmentioning

confidence: 89%

Recent advances in protein methylation: Enzymatic methylation of nucleic acid binding proteins

1998

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Heterogeneous nuclear RNP protein A1, one of the major proteins in hnRNP particle (precursor for mRNA), is known to be posttranslationally arginine-methylated in vivo on residues 193, 205, 217 and 224 within the RGG box, the motif postulated to be an RNA binding domain. Possible effect of NG-arginine methyl-modification in the interaction of protein A1 to nucleic acid was investigated. The recombinant hnRNP protein A1 was in vitro methylated by the purified nuclear protein/histone-specific protein methylase I (S-adenosylmethionine:protein-arginine N-methyltransferase) stoichiometrically and the relative binding affinity of the methylated and the unmethylated protein A1 to nucleic acid was compared: Differences in their binding properties to ssDNA-cellulose, pI values and trypsin sensitivities in the presence and absence of MS2-RNA all indicate that the binding property of hnRNP protein A1 to single-stranded nucleic acid has been significantly reduced subsequent to the methylation. These results suggest that posttranslational methyl group insertion to the arginine residue reduces protein-RNA interaction, perhaps due to interference of H-bonding between guanidino nitrogen arginine and phosphate RNA.

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Histone-arginine N-methyltransferase

Springer Handbook of Enzymes

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Myelin basic protein inhibits histone-specific protein methylase I

Cited by 13 publications

References 27 publications

Inhibitory effect of arginine-derivatives from ginseng extract and basic amino acids on protein-arginine N-methyltransferase

Inhibitory effect of arginine-derivatives from ginseng extract and basic amino acids on protein-arginine N-methyltransferase

Recent advances in protein methylation: Enzymatic methylation of nucleic acid binding proteins

Histone-arginine N-methyltransferase

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