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
    • Organic Chemistry
    • Clinical Biochemistry

    Fingerprint

    Dive into the research topics of 'Recent advances in protein methylation: Enzymatic methylation of nucleic acid binding proteins'. Together they form a unique fingerprint.

    Cite this