The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684
The origin of the genetic code
Crick, F. H. C. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90392-6 · Cited by 2,320
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269
Compilation of tRNA sequences and sequences of tRNA genes
Sprinzl, M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki012 · Cited by 1,916
In Vitro Selection of Functional Nucleic Acids
Wilson, D. S., & Szostak, J. W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.611 · Cited by 1,217
Isolation of New Ribozymes from a Large Pool of Random Sequences
Bartel, D. P., & Szostak, J. W. (1993) · Science · doi:10.1126/science.7690155 · Cited by 900
DIVERSITY OF OLIGONUCLEOTIDE FUNCTIONS
Gold, L., Polisky, B. A., Uhlenbeck, O. C., & Yarus, M. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.003555 · Cited by 809
Compilation of tRNA sequences and sequences of tRNA genes
Sprinzl, M. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.148 · Cited by 750
Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures
Noller, H. F., Hoffarth, V., & Zimniak, L. (1992) · Science · doi:10.1126/science.1604315 · Cited by 728
A simple structural feature is a major determinant of the identity of a transfer RNA
Hou, Y., & SCHIMMEL, P. R. (1988) · Nature · doi:10.1038/333140a0 · Cited by 604
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–145 of 145
Katoh, T., & Suga, H. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf446 · Cited by 8
Self-citationBalke, D., Kuss, A. W., & Müller, S. (2015) · Life · doi:10.3390/life6010001 · Cited by 9
Katoh, T., & Suga, H. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae219 · Cited by 7
Self-citationLu, W., Terasaka, N., Sakaguchi, Y., Suzuki, T., Suzuki, T., & Suga, H. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae151 · Cited by 5
Self-citationPrebiotic chiral transfer from self-aminoacylating ribozymes may favor either handedness
Kenchel, J., Vázquez-Salazar, A., Wells, R., Brunton, K., Janzen, E., Schultz, K. M., Liu, Z., Li, W., Parker, E. T., Dworkin, J. P., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52362-x · Cited by 6
On the Dimerization of the Primitive tRNAs: Implications in the Origin of Genetic Code
Giménez, J. A. M., & Tabarés‐Seisdedos, R. (2002) · Journal of Theoretical Biology · doi:10.1006/jtbi.2002.3044 · Cited by 6
Mechanistic studies on acyl‐transferase ribozymes and beyond
Hodgson, D. R. W., & Suga, H. (2003) · Biopolymers · doi:10.1002/bip.10518 · Cited by 6
Self-citationPivotal Impacts of Retrotransposon Based Invasive RNAs on Evolution
Habibi, L., & Salmani, H. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01957 · Cited by 5
Aminoacyl-tRNA synthetases: a complex system beyond protein synthesis
Bori-Sanz, T., Guitart, T., & de Pouplana, L. R. (2006) · RACO (Revistes Catalanes amb Accés Obert) (Consorci de Serveis Universitaris de Catalunya) · doi:10.2436/cs.v0i0.350 · Cited by 5
Saito, H., Yamada, A., Ohmori, R., Kato, Y., Yamanaka, T., Yoshikawa, K., & Inoue, T. (2007) · International Symposium on Micro-NanoMechatronics and Human Science · doi:10.1109/mhs.2007.4420868 · Cited by 5
Self-citationKöhrer, C., & RajBhandary, U. L. (2009) · Nucleic acids and molecular biology · doi:10.1007/978-3-540-70941-1_7 · Cited by 4
Some introductory formalizations on the affine Hilbert spaces model of the origin of life
Balázs, A. (2006) · Biosystems · doi:10.1016/j.biosystems.2005.12.005 · Cited by 4
Higuchi, T., & Suga, H. (2010) · Journal of Synthetic Organic Chemistry Japan · doi:10.5059/yukigoseikyokaishi.68.217 · Cited by 4
Self-citationCharacterization of Novel Functions and Topologies in RNA
Burton, A. S. (2000) · doi:10.15760/etd.363 · Cited by 4
Expanding the Scope of Ribosome‐Mediated Biosynthesis in vitro using tRNA‐Aminoacylating Ribozyme
Cho, N., Jin, H., Jeon, H., Lee, K., & Lee, J. (2024) · Israel Journal of Chemistry · doi:10.1002/ijch.202300174 · Cited by 3
Aminoacyl-tRNA Synthetases as Clues to Establishment of the Genetic Code
de Pouplana, L. R., & SCHIMMEL, P. R. (2007) · Springer eBooks · doi:10.1007/0-387-26887-1_8 · Cited by 3
Ayukawa, S., Enomoto, T., & Kiga, D. (2019) · Springer eBooks · doi:10.1007/978-981-13-3639-3_6 · Cited by 3
Metal Ion Requirements in Artificial Ribozymes that Catalyze Aminoacylation and Redox Reactions
Suga, H., Futai, K., & Jin, K. (2011) · Royal Society of Chemistry eBooks · doi:10.1039/9781849732512-00277 · Cited by 2
Self-citationDevelopment of Flexizyme Aminoacylation Ribozymes and Their Applications
Katoh, T., Goto, Y., Passioura, T., & Suga, H. (2021) · doi:10.1002/9783527814527.ch20 · Cited by 2
Self-citationHegazy, U. M., & Mannervik, B. (2009) · doi:10.1002/9783527631780.ch9 · Cited by 2
Functional Analysis of Histidine‐Dependent Self‐Cleaving RNAs Obtained by In Vitro Selection
Sakimoto, N., Tanaka, S. A., Hatakenaka, R., Yamaguchi, Y., Tomita‐Sudo, E., Akita, T., Ishigaki, T., Iwai, S., & Kawakami, J. (2025) · ChemBioChem · doi:10.1002/cbic.202500411 · Cited by 1
A synthetic approach for protein evolution and cell engineering
Saito, H., Inoue, T., & Shiba, K. (2006) · International Symposium on Micro-NanoMechatronics and Human Science · doi:10.1109/mhs.2006.320321 · Cited by 1
Self-citationLau, M. W. L., & Ferré-D’Amaré, A. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10058-6 · Cited by 1
Synthetic Expansion of the Central Dogma
Sisido, M. (2007) · Chemical biology · doi:10.1002/9783527619375.ch5 · Cited by 1
Rogers, J. M., & Suga, H. (2019) · Wiley eBooks · doi:10.1002/9783527823987.vol2_c15 · Cited by 1
Self-citationJanzen, E., Shen, Y., Liu, Z., Blanco, C., & Chen, I. A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.14.444235 · Cited by 1
Nucleotides and Nucleic Acids; Oligo- and Polynucleotides
Loakes, D. (2010) · Royal Society of Chemistry eBooks · doi:10.1039/9781849730839-00144 · Cited by 1
Shirokikh, N. E. (2023) · Preprints.org · doi:10.20944/preprints202305.0415.v1 · Cited by 1
Thermosynthesis as energy source for the RNA World: a new model for the origin of lifePreprint
Muller, A. W. J. (2005) · arXiv (Cornell University) · doi:10.48550/arxiv.q-bio/0501013
Drug discovery of non-standard peptide with genetic code reprogramming
Yamaguchi, A., Katoh, T., & Suga, H. (2011) · Drug Delivery System · doi:10.2745/dds.26.584
Self-citationSynthetic RNA Technologies to Control Functions of Mammalian Cells
Saito, H. (2015) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.14-00240-4
Self-citationDiscovery of Human MicroRNA Precursor Binding to Folic Acid by Small RNA Transcriptomic SELEX
Terasaka, N. (2017) · Springer theses · doi:10.1007/978-4-431-56517-8_2
Orthogonal Ribosome–tRNAs Pair by Engineering of Peptidyl Transferase Center
Terasaka, N. (2017) · Springer theses · doi:10.1007/978-4-431-56517-8_3
RNA Rings in the Origin of Life
Moreira, A. (2003) · ResearchSpace (University of Auckland)
Maghami, M. G. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8152
Cyclic Peptides as Chemical Probes
Serrano, L., Roper, G., & Kawamura, A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160745-00100
Expanding Chemical and Structural Space in mRNA Display
Liu, M. (2021) · Utrecht University Repository (Utrecht University) · doi:10.33540/788
Terasaka, N. (2017) · Springer theses · doi:10.1007/978-4-431-56517-8_4
Suga, H. (2003) · Kobunshi · doi:10.1295/kobunshi.52.144
Self-citationTerasaka, N. (2017) · Springer theses · doi:10.1007/978-4-431-56517-8_1
Lau, M. W. L., & Ferré-D’Amaré, A. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.10058-6
A reprogrammed genetic code consisting of 32 distinct amino acids
Katoh, T., & Suga, H. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag140
Self-citationKosugi, H., Nakanishi, H., Hayashi, G., & Murakami, H. (2026) · ChemBioChem · doi:10.1002/cbic.70375
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
