Aminoacyl-tRNA synthetase mutants degrade protein at a normal rate.
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.
D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics* / Q000378:metabolism; D002478:Cells, Cultured; D007700:Kinetics; D009154:Mutation; D011506:Proteins / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D013696:Temperature
D011506:Proteins; D012346:RNA, Transfer, Amino Acyl; D000604:Amino Acyl-tRNA Synthetases