Hydrodynamic properties and structure of the rat liver 12 S arginyl- and lysyl-tRNA synthetase complex.
Eukaryotic aminoacyl-tRNA synthetases occur in multienzyme complexes in contrast to their prokaryotic counterparts. A core 12 S rat liver complex (Mr 290,000) was recently purified to homogeneity consisting of two polypeptides with Mr 73,000 and 65,000 identified as lysyl- and arginyl-tRNA synthetase, respectively (Dang et al. (1982) Biochemistry 21,1959-1966). Using the modified hydrodynamic theory of Kirkwood (Kirkwood, J.R. (1954) J. Polym. Sci. 12,1-14), we have determined that the model most consistent with the hydrodynamic properties of the 12 S complex is a tetrameric tetrahedral model.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008099:Liver / Q000201:enzymology*; D008250:Lysine-tRNA Ligase / Q000378:metabolism*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000378:metabolism*; D051381:Rats
D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase; D008250:Lysine-tRNA Ligase