ArticleJournal of the American Chemical Society2015
Evolving tRNA(Sec) for efficient canonical incorporation of selenocysteine.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 70 citations in OpenAlex.
- Reassigning an amber codon to selenocysteine using a functional cysteine suppression pair inSynthetic and systems biotechnology · 2027Article
- Pyrrolysine Aminoacyl-tRNA Synthetase as a Tool for Expanding the Genetic Code.International journal of molecular sciences · 2025Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Incorporation of Multiple βACS central science · 2024Article
- Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- tRNA engineering strategies for genetic code expansion.Frontiers in genetics · 2024Review
- Non-standard amino acid incorporation into thiol dioxygenases.Methods in enzymology · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Suppressor tRNAs at the interface of genetic code expansion and medicine.Frontiers in genetics · 2024Review
- Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023Review
- Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023Article
- Recent advances in screening amino acid overproducers.Engineering microbiology · 2023Review
- Creating Selenocysteine-Specific Reporters Using Inteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine.Nature communications · 2022Article
- Uncovering translation roadblocks during the development of a synthetic tRNA.Nucleic acids research · 2022Article
- Intein-based Design Expands Diversity of Selenocysteine Reporters.Journal of molecular biology · 2022Article
- Harnessing selenocysteine to enhance microbial cell factories for hydrogen production.Frontiers in catalysis · 2022Article
- Improving the Efficiency and Orthogonality of Genetic Code Expansion.Biodesign research · 2022Review
- Using selenocysteine-specific reporters to screen for efficient tRNAMethods in enzymology · 2022Article
- Heat adaptation of phage T7 under an extended genetic code.Virus evolution · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial selenocysteine incorporation occurs in response to opal stop codons and is dependent on the presence of a selenocysteine insertion sequence (SECIS) element, which recruits the selenocysteine specific elongation factor and tRNA(Sec) needed to reassign the UGA codon. The SECIS element is a stem-loop RNA structure immediately following the UGA codon and forms part of the coding sequence in bacterial selenoproteins. Although the site specific incorporation of selenocysteine is of great interest for protein engineering, the sequence constraints imposed by the adjoining SECIS element severely limit its use. We have evolved an E. coli tRNA(Sec) that is compatible with the canonical translation machinery and can suppress amber stop codons to incorporate selenocysteine with high efficiency. This evolved tRNA(Sec) allows the production of new recombinant selenoproteins containing structural motifs such as selenyl-sulfhydryl and diselenide bonds.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.