ArticleRSC advances2018
Chemically-defined lactose-based autoinduction medium for site-specific incorporation of non-canonical amino acids into proteins.
Article in RSC advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Article
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- A novel sustainable platform for scaled manufacturing of double-stranded RNA biopesticides.Bioresources and bioprocessing · 2022Article
- Rebooting life: engineering non-natural nucleic acids, proteins and metabolites in microorganisms.Microbial cell factories · 2022Review
- Expanding the Scope of Orthogonal Translation with Pyrrolysyl-tRNA Synthetases Dedicated to Aromatic Amino Acids.Molecules (Basel, Switzerland) · 2020Article
- Overcoming Near-Cognate Suppression in a Release Factor 1-Deficient Host with an Improved Nitro-Tyrosine tRNA Synthetase.Journal of molecular biology · 2020Article
- Unexpected implications of STAT3 acetylation revealed by genetic encoding of acetyl-lysine.Biochimica et biophysica acta. General subjects · 2019Article
- Reconstitution of Mammalian Enzymatic Deacylation Reactions in Live Bacteria Using Native Acylated Substrates.ACS synthetic biology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genetic code expansion technology enables the site-specific incorporation of dozens of non-canonical amino acids (NCAAs) into proteins expressed in live cells. The NCAAs can introduce various chemical functionalities into proteins, ranging from natural post-translational modifications, to spectroscopic probes and chemical handles for bioorthogonal reactions. These chemical groups provide powerful tools for structural, biochemical, and biophysical studies, which may require significant quantities of recombinantly expressed proteins. NCAAs are usually encoded by an in-frame stop codon, such as the TAG (amber) stop codon, which leads to the expression of C-terminally truncated proteins. In addition, the incubation medium should be supplemented with the NCAA at a final concentration of 1-10 mM, which may be challenging when the availability of the NCAA is limited. Hence, bacterial expression of proteins carrying NCAAs can benefit from improvement in protein yield per given amount of added NCAA. Here, we demonstrate the applicability of an optimized chemically-defined lactose-based autoinduction (AI) medium to the expression of proteins carrying a NCAA, using the archaeal pyrrolysyl-tRNA synthetase/tRNA pair from the
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Registered trials
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