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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Martinis SA,Boniecki MTdoi
10.1016/j.febslet.2009.11.071subject
Has Abstractpub_date
2010-01-21 00:00:00pages
455-9issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00984-3journal_volume
584pub_type
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