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An in vitro evolved precursor tRNA with aminoacylation activity
Open accessAbstract
A set of catalysts for aminoacyl-tRNA synthesis is an essential component for translation. The RNA world hypothesis postulates that RNA catalysts could have played this role. Here we show an in vitro evolved precursor tRNA consisting of two domains, a catalytic 5'-leader sequence and an aminoacyl-acceptor tRNA. The 5'-leader sequence domain selectively self-charges phenylalanine on the 3'-terminus of the tRNA domain. This cis-acting ribozyme is susceptible to RNase P RNA, generating the corresponding 5'-leader segment and the mature tRNA. Moreover, the 5'-leader segment is able to aminoacylate the mature tRNA in trans. Mutational studies have revealed that C(74) and C(75) at the tRNA aminoacyl-acceptor end form base pairs with G71 and G70 of the trans-acting ribozyme. Such Watson-Crick base pairing with tRNA has been observed in RNase P RNA and 23S rRNA, suggesting that all three ribozymes use a similar mechanism for the recognition of the aminoacyl-acceptor end. Our demonstrations indicate that catalytic precursor tRNAs could have provided the foundations for the genetic coding system in the proto-translation system.
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“Artificial selections have identified ribozymes capable of aminoacylating their own sequence or other sequences (and tRNAs) in trans at specific sites, using a variety of activated amino acids or modified precursors (Figure 3A) [180–185].”
From The RNA world as a model system to study the origin of life (2015) · cites this paper as [183]
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Metadata
- Authors
- Saito, H., Kourouklis, D., & Suga, H.
- Affiliations
- University at Buffalo, State University of New York (US)
- Corresponding author
- Suga, Hiroaki
- Venue
- The EMBO Journal
- Published
- 2001-04-02
- Volume
- 20
- Issue
- 7
- Pages
- 1797-1806
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC145511
- OpenAlex
- W2029181479
- Cited by
- 145
- References
- 55
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 8 · 2023: 7 · 2022: 4 · 2021: 5 · 2020: 6 · 2019: 6 · 2018: 4 · 2017: 9 · 2016: 5 · 2015: 5 · 2014: 4 · 2013: 2 · 2012: 2
- FWCI
- 2.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Japan Society for the Promotion of Science
- National Institute of General Medical Sciences (GM-59159, R01GM059159)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- aminoacyl-tRNA synthetase, in vitro evolution, ribozymes, RNA world, aminoacylation, trans-acting ribozyme, RNase P RNA, Watson-Crick base pairing, origin of translation, origin of the genetic code
- MeSH terms
- Acylation, Base Sequence, Endoribonucleases, Molecular Sequence Data, Nucleic Acid Conformation, RNA Precursors, Mutagenesis, RNA, Catalytic, Ribonuclease P
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