The balance between pre- and post-transfer editing in tRNA synthetases.

The balance between pre- and post-transfer editing in tRNA synthetases.
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DOI:
10.1016/j.febslet.2009.11.071
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发表时间:
2010-01-21
期刊:
影响因子:
3.5
通讯作者:
Boniecki MT
Boniecki MT
中科院分区:
生物学3区
文献类型:
--
作者:
Martinis SA;Boniecki MT

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TRNA氨基酰化的保真度在一定程度上依赖于氨基酸编辑机制。清除错误荷电的tRNA的水解活性通常位于tRNA合成酶上的活性部位,该活性部位不同于其合成的氨酰化活性部位。还可以激活对tRNA合成酶氨基酰基腺苷酸酯中间体进行水解的第二预转移编辑途径。转移前和转移后的编辑活动可以在单个tRNA合成酶中共存,从而导致保真度机制的冗余。然而,在大多数情况下,一条途径似乎是主导的,但当受到损害时,第二条途径可以被激活以抑制tRNA合成酶的不忠诚。
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.
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