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Heterogeneous nuclear RNP protein A1‐arginine methylation during HCT‐48 cell cycle
Author(s) -
Park Seung Hee,
Park Gil Hong,
Gu Hyunmin,
Hwang WooIk,
Lim In Kyoung,
Paik Woon Ki,
Kim Sangduk
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203071
Subject(s) - methylation , methyltransferase , protein arginine methyltransferase 5 , protein methylation , arginine , endogeny , biochemistry , chemistry , enzyme , microbiology and biotechnology , cell cycle , biology , cell , amino acid , dna
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 NG‐monomethylarginine and NG,NG‐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.