Autophosphorylation of degradation products of arginyl-tRNA synthetase protein, isolated from Bom:NMRI mouse liver.
Proteins of M(r) 140, 60, 57, 50, 22, and 14 kDa, all possessing arginyl-tRNA synthetase activity, were subjected to phosphorylation without addition of exogenous protein kinase activity. All proteins except the 14 kDa were shown to contain endogenous protein kinase activity. The product of autophosphorylation of the 60, 57, 50, and 22 kDa proteins was identified as a phosphorylated 14.9 kDa molecule. In some cases higher molecular weight phosphorylated proteins were also detected. Properties of the 60 kDa species are described.
Berg
B H
BH
Department of Biochemistry and Molecular Biology, University of Bergen, Norway.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology*; D051379:Mice; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D012347:RNA, Transfer, Arg
D010446:Peptide Fragments; D012347:RNA, Transfer, Arg; D010769:Phosphothreonine; D010768:Phosphoserine; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D001126:Arginine-tRNA Ligase