Altered aminoacyl-tRNA synthetase complexes in CHO cell mutants.
The Chinese hamster ovary (CHO) aminoacyl-tRNA synthetase mutants Gln-2, His-1, and Lys-101 were analyzed for alterations in respective particulate enzyme forms. The mutant Gln-2 showed a preferential loss of the lower molecular weight enzyme form for glutamine. His-1 showed alterations of the enzyme complexes for several other aminoacyl-tRNA activities but only decreased activity for itself. The mutant Lys-101 only showed an altered Lysyl-tRNA synthetase. These results provide evidence for a model of the intracellular role of the aminoacyl-tRNA synthetase complexes wherein the high molecular weight forms utilize amino acids directly from the extracellular pool while the low molecular weight forms utilize intracellular pools.
D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics*; D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D005260:Female; D046911:Macromolecular Substances; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000235:genetics; D009154:Mutation
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases