Clark J L, Rabe J, Arfin S M
J Cell Physiol. 1979 Jan;98(1):237-9. doi: 10.1002/jcp.1040980125.
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.
在野生型CHO细胞中,快速降解和缓慢降解的蛋白质的稳定性在允许温度和非允许温度下都与三种温度敏感型氨酰-tRNA合成酶突变体中的相似,尽管合成酶突变体中tRNA的负载程度随温度有很大差异。这些结果表明,在真核系统的各种生理条件下观察到的蛋白质分解速率的改变不是由未负载的tRNA介导的。