Journal
NATURE CHEMICAL BIOLOGY
Volume 16, Issue 6, Pages 702-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41589-020-0500-6
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Funding
- Japan Society for the Promotion of Science (JSPS) [26220204]
- Human Frontier Science Program [RGP0015/2017]
- Japan Science and Technology (JST) agency
- CREST-Molecular Technology [JPMJCR12L2]
- JSPS [26560429]
- [12J08188]
- [19K16200]
- [JP16J04031]
- Grants-in-Aid for Scientific Research [26560429] Funding Source: KAKEN
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When the primitive translation system first emerged in the hypothetical RNA world, ribozymes could have been responsible for aminoacylation. Given that naturally occurring T-box riboswitches selectively sense the aminoacylation status of cognate tRNAs, we introduced a domain of random sequence into a T-box-tRNA conjugate and isolated ribozymes that were self-aminoacylating on the 3'-terminal hydroxyl group. One of them, named Tx2.1, recognizes the anticodon and D-loop of tRNA via interaction with its stem I domain, similarly to the parental T-box, and selectively charges N-biotinyl-L-phenylalanine (Bio-(L)Phe) onto the 3' end of the cognate tRNA in trans. We also demonstrated the ribosomal synthesis of a Bio-(L)Phe-initiated peptide in a Tx2.1-coupled in vitro translation system, in which Tx2.1 catalyzed specific tRNA aminoacylation in situ. This suggests that such ribozymes could have coevolved with a primitive translation system in the RNA world.
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