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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Martinis SA,Boniecki MT

doi

10.1016/j.febslet.2009.11.071

subject

Has Abstract

pub_date

2010-01-21 00:00:00

pages

455-9

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00984-3

journal_volume

584

pub_type

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