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Enzymatic methylation of recombinant TIS21 protein‐arginine residues
Author(s) -
Lim Kyoung,
Park TaeJun,
Kim Sangduk,
Lee Hyang Woo,
Paik Woon Ki
Publication year - 1998
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 - 10.1002/iub.7510450504
Subject(s) - methylation , recombinant dna , biochemistry , arginine , fusion protein , microbiology and biotechnology , escherichia coli , protein methylation , chemistry , peptide , complementary dna , amino acid , enzyme , expression vector , biology , methyltransferase , gene
Recombinant TIS21 protein was overexpressed in Escherichia coli harboring the expression vector plasmid pQE‐30 carrying the TIS21 cDNA coding sequence containing an extra 120 nucleotides upstream. Employing this protein consisting of 158 amino acid residues of the main chain plus 40 residues of the fusion peptide, It was found that one of the protein methylase I group [S‐adenosylmethionine:nuclear protein/histone‐arginine N‐methyltransferase; EC 2.1.1.23; J. Biol. Chem., 269 , 1075 (1994)] methylated this protein. The methylation products were identified as guanidino‐N‐methylated arginines. Some of the kinetics of the reaction are described.