ArticleProtein science : a publication of the Protein Society2010
Genetic encoding of non-natural amino acids in Drosophila melanogaster Schneider 2 cells.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 36 citations in OpenAlex.
- Making Sense of "Nonsense" and More: Challenges and Opportunities in the Genetic Code Expansion, in the World of tRNA Modifications.International journal of molecular sciences · 2022Review
- Article
- Therapeutic applications of genetic code expansion.Synthetic and systems biotechnology · 2018Review
- The central role of tRNA in genetic code expansion.Biochimica et biophysica acta. General subjects · 2017Review
- A molecular engineering toolbox for the structural biologist.Quarterly reviews of biophysics · 2017Review
- Genetic code expansion for multiprotein complex engineering.Nature methods · 2016Article
- Improved Incorporation of Noncanonical Amino Acids by an Engineered tRNA(Tyr) Suppressor.Biochemistry · 2016Article
- Expanding the genetic code of Drosophila melanogaster.Nature chemical biology · 2012Article
- Codon reassignment in the Escherichia coli genetic code.Nucleic acids research · 2010Article
- Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion.Nucleic acids research · 2010Article
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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
Insect cells are useful for the high-yield production of recombinant proteins including chemokines and membrane proteins. In this study, we developed an insect cell-based system for incorporating non-natural amino acids into proteins at specific sites. Three types of promoter systems were constructed, and their efficiencies were compared for the expression of the prokaryotic amber suppressor tRNA(Tyr) in Drosophila melanogaster Schneider 2 cells. When paired with a variant of Escherichia coli tyrosyl-tRNA synthetase specific for 3-iodo-L-tyrosine, the suppressor tRNA transcribed from the U6 promoter most efficiently incorporated the amino acid into proteins in the cells. The transient and stable introductions of these prokaryotic molecules into the insect cells were then compared in terms of the yield of proteins containing non-natural amino acids, and the "transient" method generated a sevenfold higher yield. By this method, 4-azido-L-phenylalanine was incorporated into human interleukin-8 at a specific site. The yield of the azido-containing IL-8 was 1 microg/1 mL cell culture, and the recombinant protein was successfully labeled with a fluorescent probe by the Staudinger-Bertozzi reaction.
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