Aminoacyl-tRNA synthetase mutants degrade protein at a normal rate
- 1 January 1979
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 98 (1), 237-239
- https://doi.org/10.1002/jcp.1040980125
Abstract
The stability of both rapidly and slowly degraded proteins in wild type CHO cells is similar to that in three ts aminoacyl‐tRNA synthetase mutants at both permissive and non‐permissive temperatures, although the degree of tRNA charging in the synthetase mutants differs considerably with temperature. These results indicate that the altered rate of protein breakdown seen under a variety of physiological conditions in eukaryotic systems is not mediated by uncharged tRNA.This publication has 9 references indexed in Scilit:
- [20] Methods for determining the extent of tRNA aminoacylation in vivo in cultured mammalian cellsMethods in Enzymology, 1979
- Effect of extreme amino acid starvation on the protein synthetic machinery of CHO cellsJournal of Cellular Physiology, 1978
- Biochemical characterization of a mutant asparaginyl-tRNA synthetase from Chinese hamster ovary cells.Published by Elsevier ,1978
- CHO cell mutants for arginyl-, asparagyl-, glutaminyl-, histidyl- and methionyl-transfer RNA synthetases: Identification and initial characterizationCell, 1977
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- Requirement for protein synthesis in the regulation of protein breakdown in cultured hepatoma cellsBiochemistry, 1975
- Control of Initiation of Protein Synthesis in Human CellsJournal of Biological Chemistry, 1973
- Protein Degradation in Cultured CellsPublished by Elsevier ,1973
- A Role of Aminoacyl-tRNA in the Regulation of Protein Breakdown in Escherichia coliProceedings of the National Academy of Sciences, 1971