title: The balance between pre- and post-transfer editing in tRNA synthetases.
abstract: The 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.
authors: Department of Biochemistry, University of Illinois at Urbana-Champaign, 419 Roger Adams Laboratory, Box B-4, 600 S. Mathews Ave., Urbana, IL 61801, United States. martinis@uiuc.edu
authors: Susan A
authors: SA
authors: Martinis
authors: Michal T
authors: MT
authors: Boniecki
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D017393:RNA Editing; D012343:RNA, Transfer / Q000378:metabolism*; D046249:Transfer RNA Aminoacylation
chemical_list: D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases