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Altered aminoacyl‐tRNA synthetase complexes in CHO cell mutants
Author(s) -
Pahuski Eddie,
Klekamp Mark,
Condon Tom,
Hampel A. E.
Publication year - 1983
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041140114
Subject(s) - chinese hamster ovary cell , aminoacyl trna synthetase , mutant , biochemistry , transfer rna , enzyme , intracellular , glutamine synthetase , amino acid , biology , amino acyl trna synthetases , glutamine , protein biosynthesis , chemistry , rna , gene , receptor
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.