Altered aminoacyl-tRNA synthetase complexes in CHO cell mutants

✍ Scribed by Eddie Pahuski; Mark Klekamp; Tom Condon; A. E. Hampel

• Book ID: 102882320
• Publisher: John Wiley and Sons
• Year: 1983
• Tongue: English
• Weight: 545 KB
• Volume: 114
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041140114

✦ Synopsis

The Chinese hamster ovary (CHO) aminoacyl-tRNA synthetase mutants Gln-2, His-I, 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-I 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.