Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m¹G37.
Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m¹G37.
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DOI：
10.3390/biom7010032
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发表时间：
2017-03-21
期刊：
影响因子：
5.5
通讯作者：
Yokoyama S
中科院分区：
文献类型：
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作者：
Goto-Ito S;Ito T;Yokoyama S
转移RNA（tRNA）中第37位鸟苷的N1原子在真核生物和古细菌中被tRNA甲基转移酶5（Trm 5）甲基化，在细菌中被tRNA甲基转移酶D（TrmD）甲基化。由此产生的修饰核苷酸m1G37正调控tRNA的氨酰化，同时起到防止核糖体上+1移码的作用。有趣的是，Trm5和TrmD具有完全不同的起源，因此具有不同的三级折叠。在这篇综述中，我们描述了Trm5和TrmD利用不同的策略来识别它们的底物tRNA，主要是基于它们与底物tRNA复合的晶体结构。
The N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome. Interestingly, Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. In this review, we describe the different strategies utilized by Trm5 and TrmD to recognize their substrate tRNAs, mainly based on their crystal structures complexed with substrate tRNAs.