title: Protein arginine allylation and subsequent fluorophore targeting.
abstract: Protein allylation and fluorophore targeting: Arginine residues of the yeast nuclear ribonucleoprotein Npl3 were extensively modified by Hmt1-catalyzed allylation reaction with allyl-SAM as the allyl group donor. The allylated protein was further treated with tetrazole compounds under UV irradiation, leading to formation of protein-attached fluorescent products.
authors.affiliation: Division of Biotechnology, Dalian Institute of Chemical Physics, China.
authors.forename: Yixin
authors.initials: Y
authors.lastname: Zhang
authors.forename: Yanbo
authors.initials: Y
authors.lastname: Pan
authors.forename: Wei
authors.initials: W
authors.lastname: Yang
authors.forename: Wujun
authors.initials: W
authors.lastname: Liu
authors.forename: Hanfa
authors.initials: H
authors.lastname: Zou
authors.forename: Zongbao K
authors.initials: ZK
authors.lastname: Zhao
mesh_terms: D001120:Arginine / Q000737:chemistry*; D002384:Catalysis; D004591:Electrophoresis, Polyacrylamide Gel; D005456:Fluorescent Dyes / Q000737:chemistry*; D015394:Molecular Structure; D011484:Protein-Arginine N-Methyltransferases / Q000737:chemistry*; D012261:Ribonucleoproteins / Q000737:chemistry; D013777:Tetrazoles / Q000737:chemistry
chemical_list: D005456:Fluorescent Dyes; D012261:Ribonucleoproteins; D013777:Tetrazoles; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases
keywords: S-adenosyl-L-methionine; bioorthogonal reaction; cycloaddition; fluorescence labeling; methyltransferase; protein methylation