A tRNA modification with aminovaleramide facilitates AUA decoding in protein synthesis

IF 12.9 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Nature chemical biology Pub Date : 2024-09-19 DOI:10.1038/s41589-024-01726-x

Kenjyo Miyauchi, Satoshi Kimura, Naho Akiyama, Kazuki Inoue, Kensuke Ishiguro, Thien-Son Vu, Veerasak Srisuknimit, Kenta Koyama, Gosuke Hayashi, Akiko Soma, Asuteka Nagao, Mikako Shirouzu, Akimitsu Okamoto, Matthew K. Waldor, Tsutomu Suzuki

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Abstract

Modified tRNA anticodons are critical for proper mRNA translation during protein synthesis. It is generally thought that almost all bacterial tRNAs^Ile use a modified cytidine—lysidine (L)—at the first position (34) of the anticodon to decipher the AUA codon as isoleucine (Ile). Here we report that tRNAs^Ile from plant organelles and a subset of bacteria contain a new cytidine derivative, designated 2-aminovaleramididine (ava²C). Like L34, ava²C34 governs both Ile-charging ability and AUA decoding. Cryo-electron microscopy structural analyses revealed molecular details of codon recognition by ava²C34 with a specific interaction between its terminal amide group and an mRNA residue 3′-adjacent to the AUA codon. These findings reveal the evolutionary variation of an essential tRNA modification and demonstrate the molecular basis of AUA decoding mediated by a unique tRNA modification.

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用氨基戊酰胺修饰 tRNA 可促进蛋白质合成中的 AUA 解码

修饰的 tRNA 反密码子对于蛋白质合成过程中 mRNA 的正常翻译至关重要。一般认为，几乎所有细菌的 tRNAsIle 都在反密码子的第一个位置（34）使用修饰胞苷苷（L）来将 AUA 密码子破译为异亮氨酸（Ile）。在这里，我们报告了来自植物细胞器和一部分细菌的 tRNAsIle 含有一种新的胞苷衍生物，被命名为 2-氨基戊酰胺苷（ava2C）。与 L34 一样，ava2C34 也控制着 Ile 的充电能力和 AUA 解码。冷冻电镜结构分析揭示了ava2C34识别密码子的分子细节，其末端酰胺基团与AUA密码子相邻3′的mRNA残基之间存在特异性相互作用。这些发现揭示了一种重要的 tRNA 修饰的进化变异，并证明了由一种独特的 tRNA 修饰介导的 AUA 解码的分子基础。

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来源期刊

Nature chemical biology 生物-生化与分子生物学

CiteScore

23.90

自引率

1.40%

发文量

238

审稿时长

12 months

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