Universal rules and idiosyncratic features in tRNA identity
Open accessAbstract
Correct expression of the genetic code at translation is directly correlated with tRNA identity. This survey describes the molecular signals in tRNAs that trigger specific aminoacylations. For most tRNAs, determinants are located at the two distal extremities: the anticodon loop and the amino acid accepting stem. In a few tRNAs, however, major identity signals are found in the core of the molecule. Identity elements have different strengths, often depend more on k cat effects than on K m effects and exhibit additive, cooperative or anti-cooperative interplay. Most determinants are in direct contact with cognate synthetases, and chemical groups on bases or ribose moieties that make functional interactions have been identified in several systems. Major determinants are conserved in evolution; however, the mechanisms by which they are expressed are species dependent. Recent studies show that alternate identity sets can be recognized by a single synthetase, and emphasize the importance of tRNA architecture and anti-determinants preventing false recognition. Identity rules apply to tRNA-like molecules and to minimalist tRNAs. Knowledge of these rules allows the manipulation of identity elements and engineering of tRNAs with switched, altered or multiple specificities.
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In E. coli, the tRNA species for 17 out of 20 amino acids are recognized by their anticodons.
“In E. coli, the tRNA species for 17 out of 20 amino acids are recognized by their anticodons [111].”
From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [111]
Initially, anticodons developed between the interactions of pre-tRNA and pre-aaRS.
“Initially, anticodons developed between the interactions of pre-tRNA and pre-aaRS [111].”
From The Origin of Prebiotic Information System in the Peptide/RNA World: A Simulation Model of the Evolution of Translation and the Genetic Code (2019) · cites this paper as [111]
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- Authors
- Giege, R., Sissler, M., & Florentz, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- ORCID
- Sissler, M.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1998-11-01
- Volume
- 26
- Issue
- 22
- Pages
- 5017-5035
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC147952
- OpenAlex
- W2057892106
- Cited by
- 769
- References
- 0
- Citations by year
- 2026: 10 · 2025: 17 · 2024: 30 · 2023: 36 · 2022: 30 · 2021: 28 · 2020: 28 · 2019: 37 · 2018: 37 · 2017: 28 · 2016: 31 · 2015: 22 · 2014: 37 · 2013: 30 · 2012: 26
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Nucleic Acids Research (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- univOAK (4 institutions : Université de Strasbourg, Université de Haute Alsace, INSA Strasbourg, Bibliothèque Nationale et Universitaire de Strasbourg) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- tRNA identity, aminoacylation, tRNA synthetase, anticodon loop, cognate recognition, genetic code, catalytic efficiency
- MeSH terms
- Amino Acyl-tRNA Synthetases, Genetic Code, Humans, Kinetics, Models, Molecular, Nucleic Acid Conformation, RNA, Transfer, RNA, Transfer, Amino Acyl, Protein Biosynthesis, Evolution, Molecular
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