Uncoupling of amino acid turnover on transfer RNA from protein synthesis in HeLa cells.
The aminoacylation of tRNA has been investigated in relation to protein aynthesis in living HeLa cells. In cells growing normally, the rates of tRNA charing are compatible with the observed entry of amino acids into protein. In contrast, when protein synthesis is inhibited 95--98% by either reduced temperature or cycloheximide, aminoacylation of tRNA is relatively unaffected. We conclude that, under these conditions, the aminoacylation of tRNA is uncoupled from subsequent steps in protein synthesis. These results provide for the first time a possible biological role for the observed aminoacyl-tRNA hydrolase activities of the tRNA synthetases.
D000596:Amino Acids / Q000378:metabolism*; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D003513:Cycloheximide / Q000494:pharmacology; D006367:HeLa Cells / Q000378:metabolism; D007700:Kinetics; D008566:Membranes / Q000378:metabolism; D008861:Microsomes / Q000378:metabolism; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000096:biosynthesis; D012343:RNA, Transfer / Q000378:metabolism*; D012995:Solubility; D013696:Temperature
D000596:Amino Acids; D011498:Protein Precursors; D012343:RNA, Transfer; D003513:Cycloheximide; D000604:Amino Acyl-tRNA Synthetases