title: Arginyl-tRNA synthetase from Escherichia coli affinity labeling with 3'-oxidized tRNA(Arg).
abstract: The covalent modification of E. coli arginyl-tRNA synthetase by the 2',3'-dialdehyde derivative of tRNA(Arg) (tRNA(oxArg)) resulted in the complete inactivation of the ATP-PPi exchange and aminoacylation activities of the enzyme. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the ArgRS-tRNA(oxArg) covalent complexes indicated that two bands simultaneously appeared on the gel parallel with inactivation corresponding to different higher molecular weights. This result was different from that of the other aminoacyl-tRNA synthetase labeling systems as previously reported. Upon the ribonuclease treatment of the modified ArgRS, less than 15% of both the initial ATP-PPi exchange and aminocylation activities were recovered. During the whole process of labeling and RNase treatment, the two activities of the enzyme were closely associated.
authors.affiliation: Shanghai Institute of Biochemistry, Academia Sinica, PRC.
authors.forename: X D
authors.initials: XD
authors.lastname: Cheng
authors.forename: S X
authors.initials: SX
authors.lastname: Lin
authors.forename: J P
authors.initials: JP
authors.lastname: Shi
authors.forename: Y L
authors.initials: YL
authors.lastname: Wang
mesh_terms: D000345:Affinity Labels; D001126:Arginine-tRNA Ligase / Q000378:metabolism*; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D012329:RNA, Bacterial; D012347:RNA, Transfer, Arg; D012545:Schiff Bases
chemical_list: D000345:Affinity Labels; D012329:RNA, Bacterial; D012347:RNA, Transfer, Arg; D012545:Schiff Bases; D001126:Arginine-tRNA Ligase