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The balance between pre- and post-transfer editing in tRNA synthetases Martinis SA; Boniecki MTFEBS Lett 2010[Jan]; 584 (2): 455-9The fidelity of tRNA aminoacylation is dependent in part on amino acid editing mechanisms. A hydrolytic activity that clears mischarged tRNAs typically resides in an active site on the tRNA synthetase that is distinct from its synthetic aminoacylation active site. A second pre-transfer editing pathway that hydrolyzes the tRNA synthetase aminoacyl adenylate intermediate can also be activated. Pre- and post-transfer editing activities can co-exist within a single tRNA synthetase resulting in a redundancy of fidelity mechanisms. However, in most cases one pathway appears to dominate, but when compromised, the secondary pathway can be activated to suppress tRNA synthetase infidelities.|*RNA Editing[MESH]|*Transfer RNA Aminoacylation[MESH]|Amino Acyl-tRNA Synthetases/*metabolism[MESH]|RNA, Transfer/*metabolism[MESH] |
