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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids.

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.[1]

References

  1. Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids. Link, A.J., Vink, M.K., Agard, N.J., Prescher, J.A., Bertozzi, C.R., Tirrell, D.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
 
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