Altered aminoacyl‐tRNA synthetase complexes in CHO cell mutants
- 1 January 1983
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 114 (1), 82-87
- https://doi.org/10.1002/jcp.1041140114
Abstract
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.This publication has 28 references indexed in Scilit:
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