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

Sangduk Kim, G. H. Park, W. K. Paik

Research output: Contribution to journalReview articlepeer-review

22 Citations (Scopus)

Abstract

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 N(G)-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.

Original languageEnglish
Pages (from-to)291-306
Number of pages16
JournalAmino Acids
Volume15
Issue number4
DOIs
Publication statusPublished - 1998

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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