期刊
NATURE CHEMICAL BIOLOGY
卷 6, 期 4, 页码 277-282出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.323
关键词
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资金
- Ministry of Education, Science, Sports, and Culture of Japan
- Japan Society for the Promotion of Science Fellowship
- Japan Science and Technology
- New Energy and Industrial Technology Development Organization (NEDO)
- Grants-in-Aid for Scientific Research [21115003] Funding Source: KAKEN
A modified base at the first (wobble) position of some tRNA anticodons is critical for deciphering the genetic code. In eukaryotes and eubacteria, AUA codons are decoded by tRNAs(Ile) with modified bases pseudouridine (and/or inosine) and lysidine, respectively. The mechanism by which archaeal species translate AUA codons is unclear. We describe a polyamine-conjugated modified base, 2-agmatinylcytidine (agm(2)C or agmatidine), at the wobble position of archaeal tRNA(Ile) that decodes AUA codons specifically. We demonstrate that archaeal cells use agmatine to synthesize agm(2)C of tRNA(Ile). We also identified a new enzyme, tRNA(Ile)-agm(2)C synthetase (TiaS), that catalyzes agm(2)C formation in the presence of agmatine and ATP. Although agm2C is chemically similar to lysidine, TiaS constitutes a distinct class of enzyme from tRNA(Ile)-lysidine synthetase (TilS), suggesting that the decoding systems evolved convergently across domains.
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