Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle

Seung Hee Park, Gil Hong Park, Hyunmin Gu, Woo Ik Hwang, In Kyoung Lim, Woon Ki Paik, Sangduk Kim

    Research output: Contribution to journalArticlepeer-review

    8 Citations (Scopus)


    Protein methylase I (protein-arginine N-methyltransferase) was examined in HCT-48 cells, synchronized by serum deprivation and hydroxyurea treatment. The enzyme activity to methylate the added hnRNP protein A1 increased about 2-fold from G0 to S phase, and then decreased during G2/M phase. The enzymatically [methyl-3H]-labeled hnRNP protein A1 was identified by SDS-PAGE/fluorography, and the products were identified as N(G)-monomethylarginine and N(G),N(G)-dimethyl-(asymmetric)arginines by HPLC. Among endogenous proteins, the 20-kDa species in the extract was most intensely [methyl-3H]-labeled. This 20-kDa methylation was markedly inhibited by the addition of exogenous hnRNP protein A1, indicating that these two substrates compete for the same protein methylase. The possible role of this post-translational modification has been discussed.

    Original languageEnglish
    Pages (from-to)657-666
    Number of pages10
    JournalBiochemistry and Molecular Biology International
    Issue number4
    Publication statusPublished - 1997 Jul


    • Cell cycle
    • HCT-48
    • N(G),N(G)-dimethylarginine
    • N(G)-monomethylarginine
    • Protein-arginine methyltransferase
    • S-adenosylmethionine
    • hnRNP protein A1

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Genetics


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