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Enzymatic methylation of recombinant TIS21 protein-arginine residues.

Authors
Lim, IK; Park, TJ; Kim, S; Lee, HW; Paik, WK
Citation
Biochemistry and molecular biology international, 45(5):871-878, 1998
Journal Title
Biochemistry and molecular biology international
ISSN
1039-9712
Abstract
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; BC 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.
MeSH terms
Arginine/analogs & derivatives/metabolismEscherichia coli/geneticsImmediate-Early Proteins/chemistry/isolation & purification/*metabolismMethylationProtein-Arginine N-Methyltransferases/metabolismRecombinant Proteins/chemistry/isolation & purification/metabolism
PMID
9739451
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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