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RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites
Open accessAbstract
Stop codons have been exploited for genetic incorporation of unnatural amino acids (Uaas) in live cells, but the efficiency is low possibly due to competition from release factors, limiting the power and scope of this technology. Here we show that the reportedly essential release factor 1 can be knocked out from Escherichia coli by fixing release factor 2. The resultant strain JX33 is stable and independent, and reassigns UAG from a stop signal to an amino acid when a UAG-decoding tRNA/synthetase pair is introduced. Uaas were efficiently incorporated at multiple UAG sites in the same gene without translational termination in JX33. We also found that amino acid incorporation at endogenous UAG codons is dependent on RF1 and mRNA context, which explains why E. coli tolerates apparent global suppression of UAG. JX33 affords a unique autonomous host for synthesizing and evolving novel protein functions by enabling Uaa incorporation at multiple sites.
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Cites
Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
Keiler, K. C., Waller, P. R. H., & Sauer, R. T. (1996) · Science · doi:10.1126/science.271.5251.990 · Cited by 1,125
Rewiring the keyboard: evolvability of the genetic code
Knight, R. D., Freeland, S. J., & Landweber, L. F. (2001) · Nature Reviews Genetics · doi:10.1038/35047500 · Cited by 435
Cited by
Expanding and Reprogramming the Genetic Code of Cells and Animals
Chin, J. W. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035737 · Cited by 476
Schmied, W. H., Elsässer, S. J., Uttamapinant, C., & Chin, J. W. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5069728 · Cited by 270
Histones: At the Crossroads of Peptide and Protein Chemistry
Müller, M. M., & Muir, T. W. (2015) · Chemical Reviews · doi:10.1021/cr5003529 · Cited by 247
Site-specific incorporation of phosphotyrosine using an expanded genetic code
Hoppmann, C., Wong, A., Yang, B., Li, S., Hunter, T., Shokat, K. M., & Wang, L. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2406 · Cited by 112
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Metadata
- Authors
- Johnson, D. B. F., Xu, J., Shen, Z., Takimoto, J. K., Schultz, M. D., Schmitz, R. J., Xiang, Z., Ecker, J. R., Briggs, S. P., & Wang, L.
- Venue
- Nature Chemical Biology
- Published
- 2011-09-18
- Volume
- 7
- Issue
- 11
- Pages
- 779-786
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2058079617
- Cited by
- 336
- References
- 2
- FWCI
- 9.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Johnson, D. B. F., Xu, J., Shen, Z., Takimoto, J. K., Schultz, M. D., Schmitz, R. J., Xiang, Z., Ecker, J. R., Briggs, S. P., & Wang, L. (2011). RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites. Nature Chemical Biology. https://doi.org/10.1038/nchembio.657
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