Molecular mechanism of codon recognition by tRNA species with modified uridine in the first position of the anticodon.
Open accessAbstract
Proton NMR analyses have been made to elucidate the conformational characteristics of modified nucleotides as found in the first position of the anticodon of tRNA [derivatives of 5-methyl-2-thiouridine 5'-monophosphate (pxm5s2U) and derivatives of 5-hydroxyuridine 5'-monophosphate (pxo5U)]. In pxm5s2U, the C3'-endo form is extraordinarily more stable than the C2'-endo form for the ribose ring, because of the combined effects of the 2-thiocarbonyl group and the 5-substituent. By contrast, in pxo5U, the C2'-endo form is much more stable than the C3'-endo form, because of the interaction between the 5-substituent and the 5'-phosphate group. The enthalpy differences between the C2'-endo form and the C3'-endo form have been obtained as 1.1, -0.7, and 0.1 kcal/mol (1 cal = 4.184 J) for pxm5s2U, pxo5U, and unmodified uridine 5'-monophosphate, respectively. These findings lead to the conclusion that xm5s2U in the first position of the anticodon exclusively takes the C3'-endo form to recognize adenosine (but not uridine) as the third letter of the codon, whereas xo5U takes the C2'-endo form as well as the C3'-endo form to recognize adenosine, guanosine, and uridine as the third letter of the codon on ribosome. Accordingly, the biological significance of such modifications of uridine to xm5s2U/xo5U is in the regulation of the conformational rigidity/flexibility in the first position of the anticodon so as to guarantee the correct and efficient translation of codons in protein biosynthesis.
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- Authors
- Yokoyama, S., Watanabe, T., Murao, K., Ishikura, H., Yamaizumi, Z., Nishimura, S., & Miyazawa, T.
- Affiliations
- Jichi Medical University (JP)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1985-08
- Volume
- 82
- Issue
- 15
- Pages
- 4905-4909
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC390466
- OpenAlex
- W2045979907
- Cited by
- 271
- References
- 26
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 7 · 2023: 4 · 2022: 5 · 2021: 11 · 2020: 5 · 2019: 10 · 2018: 12 · 2017: 8 · 2016: 10 · 2015: 12 · 2014: 15 · 2013: 6 · 2012: 3
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Hokkaido University
- Toray Science Foundation
- Japan Society for the Promotion of Science
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- tRNA anticodon, codon recognition, enthalpy difference, ribosome, translation (biology)
- MeSH terms
- Anticodon, Codon, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Nucleic Acid Conformation, RNA, Messenger, RNA, Transfer, Structure-Activity Relationship, Uridine
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