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The balance between pre‐ and post‐transfer editing in tRNA synthetases
Author(s) -
Martinis Susan A.,
Boniecki Michal T.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.071
Subject(s) - aminoacylation , transfer rna , amino acyl trna synthetases , aminoacyl trna synthetase , biochemistry , adenylate kinase , biology , amino acid , rna editing , chemistry , enzyme , rna , gene
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.