Identification of highly methylated arginine residues in an endogenous 20-kDa polypeptide in cancer cells

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

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


Enzymatic methylation of endogenous proteins in several cancer cell lines was investigated to understand a possible relationship between protein- arginine methylation and cellular proliferation. Cytosolic extracts prepared from several cancer cells (HeLa, HCT-48, A549, and HepG2) and incubated with S-adenosyl-L-[methyl-3H]methionine revealed an intensely [methyl-3H]- labeled 20-kDa polypeptide. On the other hand, cytosolic extracts prepared from normal colon cells did not show any methylation of the 20-kDa protein under identical conditions. To identify nature of the 20-kDa polypeptide, purified histones were methylated with HCT-48 cytosolic extracts and analyzed by SDS-PAGE. However, none of the histones comigrated with the methylated 20- kDa polypeptide, indicating that it is unlikely to be any of the histone subclasses. The [methyl-3H]group in the 20-kDa polypeptide was stable at pH 1011 (37°C for 30 min) and methylation was not stimulated by GTPγS (4 mM), thus the reaction is neither carboxyl methylesterification on isoaspartyl residues, nor on C-terminal farnesylated cysteine: The present study together with the previous identification of N(G)-methylated arginine residues in the HCT-48 cytosol fraction suggests that this novel endogenous 20-kDa arginine- methylation is a cellular proliferation-related posttranslational modification reaction.

Original languageEnglish
Pages (from-to)737-745
Number of pages9
JournalLife Sciences
Issue number8
Publication statusPublished - 1999 Jul 16
Externally publishedYes


  • 20-kDa polypeptide
  • Cell proliferation
  • Protein-arginine methylation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)


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