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Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids
Open accessAbstract
The incorporation of noncanonical amino acids into recombinant proteins in Escherichia coli can be facilitated by the introduction of new aminoacyl-tRNA synthetase activity into the expression host. We describe here a screening procedure for the identification of new aminoacyl-tRNA synthetase activity based on the cell surface display of noncanonical amino acids. Screening of a saturation mutagenesis library of the E. coli methionyl-tRNA synthetase (MetRS) led to the discovery of three MetRS mutants capable of incorporating the long-chain amino acid azidonorleucine into recombinant proteins with modest efficiency. The Leu-13 → Gly (L13G) mutation is found in each of the three MetRS mutants, and the MetRS variant containing this single mutation is highly efficient in producing recombinant proteins that contain azidonorleucine.
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Citations
Cites
Non-canonical amino acids in protein engineering
Link, A. J., Mock, M. L., & Tirrell, D. A. (2003) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2003.10.011 · Cited by 393
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Metadata
- Authors
- Link, A. J., Vink, M. K. S., Agard, N. J., Prescher, J. A., Bertozzi, C. R., & Tirrell, D. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-07-05
- Volume
- 103
- Issue
- 27
- Pages
- 10180-10185
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2106804637
- Cited by
- 189
- References
- 1
- FWCI
- 5.03
- Type
- journal article
- Language
- en
- Open access
- green
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- Link, A. J., Vink, M. K. S., Agard, N. J., Prescher, J. A., Bertozzi, C. R., & Tirrell, D. A. (2006). Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0601167103
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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