Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver. Isolation and the structural relationship of synthetase complexes.
The major high molecular weight complex of aminoacyl-tRNA synthetases is purified about 1000-fold with 30% yield from rat liver. The synthetase complex sediments at 24 S with a molecular weight of 900,000 +/- 75,000 and contains aminoacylation activities for lysine, arginine, isoleucine, leucine, methionine, glutamine, glutamate, and proline. The 24 S synthetase complex dissociates into 21 S, 18 S, 13 S, 12 S, and 10 S complexes with specific enzymatic activities. Dissociation of the 24 S complex into active free synthetases is achieved by hydrophobic interaction chromatography. The disassembly of the synthetase complex is consistent with the structural model of a heterotypic multienzyme complex and suggests that the complex formation is due to the specific intermolecular interactions among the synthetases.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases