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 journalArticle

14 Citations (Scopus)

Abstract

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
Volume65
Issue number8
DOIs
Publication statusPublished - 1999 Jul 16

Fingerprint

Methylation
Arginine
Cells
Peptides
Histones
Neoplasms
Cell Proliferation
Proteins
Post Translational Protein Processing
HeLa Cells
Cytosol
Cysteine
Polyacrylamide Gel Electrophoresis
Colon
Cell Line

Keywords

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

ASJC Scopus subject areas

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

Cite this

Identification of highly methylated arginine residues in an endogenous 20-kDa polypeptide in cancer cells. / Gu, Hyunmin; Park, Seung Hee; Park, Gil-Hong; Lim, In Kyoung; Lee, Hyang Woo; Paik, Woon Ki; Kim, Sangduk.

In: Life Sciences, Vol. 65, No. 8, 16.07.1999, p. 737-745.

Research output: Contribution to journalArticle

Gu, Hyunmin ; Park, Seung Hee ; Park, Gil-Hong ; Lim, In Kyoung ; Lee, Hyang Woo ; Paik, Woon Ki ; Kim, Sangduk. / Identification of highly methylated arginine residues in an endogenous 20-kDa polypeptide in cancer cells. In: Life Sciences. 1999 ; Vol. 65, No. 8. pp. 737-745.
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