Multiple forms of arginyl- and lysyl-tRNA synthetases in rat liver: a re-evaluation.
The size distribution of lysyl- and arginyl-tRNA synthetases in crude extracts from rat liver was re-examined by gel filtration. It is shown that irrespective of the addition or not of several proteinase inhibitors, lysyl-tRNA synthetase was present exclusively as a high-Mr entity, while arginyl-tRNA synthetase occurred as high- and low-Mr forms, in the constant proportions of 2:1, respectively. The polypeptide molecular weights of the arginyl-tRNA synthetase in these two forms were 74000 and 60000, respectively. The high-Mr forms of lysyl- and arginyl-tRNA synthetases were co-purified to yield a multienzyme complex, the polypeptide composition of which was virtually identical to that of the complexes from rabbit liver and from cultured Chinese hamster ovary cells. Of the nine aminoacyl-tRNA synthetases, specific for lysine, arginine, methionine, leucine, isoleucine, glutamine, glutamic and aspartic acids and proline, which characterize the purified complex, each, except prolyl-tRNA synthetase, was assigned to the constituent polypeptides by the protein-blotting procedure, using the previously characterized antibodies to the aminoacyl-tRNA synthetase components of the corresponding complex from sheep liver.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000302:isolation & purification*; D002850:Chromatography, Gel; D005260:Female; D008099:Liver / Q000201:enzymology*; D008250:Lysine-tRNA Ligase / Q000302:isolation & purification*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification; D051381:Rats; D011919:Rats, Inbred Strains
D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase; D008250:Lysine-tRNA Ligase