Amino Acids

, Volume 15, Issue 4, pp 291–306

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

  • Sangduk Kim
  • G. H. Park
  • W. K. Paik
Review Article


Heterogeneous nuclear RNP protein A1, one of the major proteins in hnRNP particle (precursor for mRNA), is known to be post-translationally arginine-methylatedin 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 wasin 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.


Protein-arginine methylation Nucleic acid binding protein Protein methylase I S-adenosyl-L-methionine RGG motiff 



heterogeneous ribonucleoprotein particle






myelin basic protein


high mobility group


single stranded


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Copyright information

© Springer-Verlag 1998

Authors and Affiliations

  • Sangduk Kim
    • 1
  • G. H. Park
    • 1
  • W. K. Paik
    • 2
  1. 1.Department of BiochemistryKorea University Medical School, 126Sung Buk-Gu, SeoulKorea
  2. 2.Department of BiochemistrySchool of Medicine, Ajou UniversitySuwonKorea

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