The balance between pre- and post-transfer editing in tRNA synthetases.
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.
Martinis
Susan A
SA
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
Boniecki
Michal T
MT
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D017393:RNA Editing; D012343:RNA, Transfer / Q000378:metabolism*; D046249:Transfer RNA Aminoacylation
D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases