ArticleNucleic acids research2013
Tertiary structure of bacterial selenocysteine tRNA.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- ncRNA Editing: Functional Characterization and Computational Resources.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Human selenocysteine synthase, SEPSECS, has evolved to optimize binding of a tRNA-based substrate.Nucleic acids research · 2024Article
- Isolation of nucleic acids using liquid-liquid phase separation of pH-sensitive elastin-like polypeptides.Scientific reports · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Structural basis for the selective methylation of 5-carboxymethoxyuridine in tRNA modification.Nucleic acids research · 2023Article
- Structural basis for the tRNA-dependent activation of the terminal complex of selenocysteine synthesis in humans.Nucleic acids research · 2023Article
- tRNAscan-SE 2.0: improved detection and functional classification of transfer RNA genes.Nucleic acids research · 2021Article
- Review
- Oligonucleotide-mediated tRNA sequestration enables one-pot sense codon reassignment in vitro.Nucleic acids research · 2018Article
- Challenges of site-specific selenocysteine incorporation into proteins by Escherichia coli.RNA biology · 2018Review
- Recoding of the selenocysteine UGA codon by cysteine in the presence of a non-canonical tRNARNA biology · 2018Article
- Insights into substrate promiscuity of human seryl-tRNA synthetase.RNA (New York, N.Y.) · 2017Article
- Protein-only RNase P function in Escherichia coli: viability, processing defects and differences between PRORP isoenzymes.Nucleic acids research · 2017Article
- Computational identification of the selenocysteine tRNA (tRNASec) in genomes.PLoS computational biology · 2017Article
- Article
- [Facile Recoding of Selenocysteine in Nature].Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016Article
- Facile Recoding of Selenocysteine in Nature.Angewandte Chemie (International ed. in English) · 2016Article
- Cleavage of Model Substrates by Arabidopsis thaliana PRORP1 Reveals New Insights into Its Substrate Requirements.PloS one · 2016Article
- SerRS-tRNASec complex structures reveal mechanism of the first step in selenocysteine biosynthesis.Nucleic acids research · 2015Article
- Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB.Nucleic acids research · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenocysteine (Sec) is translationally incorporated into proteins in response to the UGA codon. The tRNA specific to Sec (tRNA(Sec)) is first ligated with serine by seryl-tRNA synthetase (SerRS). In the present study, we determined the 3.1 Å crystal structure of the tRNA(Sec) from the bacterium Aquifex aeolicus, in complex with the heterologous SerRS from the archaeon Methanopyrus kandleri. The bacterial tRNA(Sec) assumes the L-shaped structure, from which the long extra arm protrudes. Although the D-arm conformation and the extra-arm orientation are similar to those of eukaryal/archaeal tRNA(Sec)s, A. aeolicus tRNA(Sec) has unique base triples, G14:C21:U8 and C15:G20a:G48, which occupy the positions corresponding to the U8:A14 and R15:Y48 tertiary base pairs of canonical tRNAs. Methanopyrus kandleri SerRS exhibited serine ligation activity toward A. aeolicus tRNA(Sec) in vitro. The SerRS N-terminal domain interacts with the extra-arm stem and the outer corner of tRNA(Sec). Similar interactions exist in the reported tRNA(Ser) and SerRS complex structure from the bacterium Thermus thermophilus. Although the catalytic C-terminal domain of M. kandleri SerRS lacks interactions with A. aeolicus tRNA(Sec) in the present complex structure, the conformational flexibility of SerRS is likely to allow the CCA terminal region of tRNA(Sec) to enter the SerRS catalytic site.
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