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Cytosine methylation of tRNA-Asp by DNMT2 has a role in translation of proteins containing poly-Asp sequences

机译：DNMT2对tRNA-Asp的胞嘧啶甲基化在翻译含有poly-Asp序列的蛋白质中起作用

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The Dnmt2 RNA methyltransferase catalyses the methylation of C38 in the anticodon loop of tRNA-Asp, but the molecular role of this methylation is unknown. Here, we report that mouse aspartyl-tRNA synthetase shows a four to fivefold preference for C38-methylated tRNA-Asp. Consistently, a 30% reduced charging level of tRNA-Asp was observed in Dnmt2 knockout (KO) murine embryonic fibroblast cells. Gene expression analysis with fluorescent reporter proteins fused to an N-terminal poly-Asp sequence showed that protein synthesis of poly-Asp-tagged reporter proteins was reduced in Dnmt2 KO cells as well. The same effect was observed with endogenous proteins containing poly-Asp sequences, indicating that Dnmt2-mediated C38 methylation of tRNA-Asp regulates the translation of proteins containing poly-Asp sequences. Gene ontology searches for proteins containing poly-Asp sequences in the human proteome showed that a significant number of these proteins have roles in transcriptional regulation and gene expression. Hence, the Dnmt2-mediated methylation of tRNA-Asp exhibits a post-transcriptional regulatory role by controlling the synthesis of a group of target proteins containing poly-Asp sequences.
机译：Dnmt2 RNA甲基转移酶催化tRNA-Asp的反密码子环中C38的甲基化，但是这种甲基化的分子作用尚不清楚。在这里，我们报告说，小鼠天冬氨酰-tRNA合成酶显示C38甲基化的tRNA-Asp有4至5倍的偏好。一致地，在Dnmt2敲除（KO）鼠胚胎成纤维细胞中观察到tRNA-Asp的充电水平降低了30％。使用与N末端poly-Asp序列融合的荧光报告蛋白进行基因表达分析，结果表明Dnmt2 KO细胞中poly-Asp标记的报告蛋白的蛋白质合成也减少了。用含有多-Asp序列的内源蛋白观察到相同的效果，表明Dnmt2介导的tRNA-Asp的C38甲基化调节含有多-Asp序列的蛋白的翻译。基因本体论搜索在人类蛋白质组中包含多Asp序列的蛋白质的过程表明，这些蛋白质中有大量在转录调控和基因表达中起作用。因此，Dnmt2介导的tRNA-Asp甲基化通过控制一组含有多Asp序列的靶蛋白的合成而显示出转录后的调控作用。

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