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Design of an S-Allylcysteine in situ production and incorporation system based on a novel pyrrolysyl-tRNA synthetase variant
Citation key 150.2016.Exner
Author Exner, M. P., and Kuenzl, T., and Schwagerus, S., and To, T., and Ouyang, Z., and Hoesl, M. G., and Lensen, M. C., and Hackenberger, C. P. R., and Panke, S., and Budisa, N.
Pages 85–90
Year 2017
DOI 10.1002/cbic.201600537
Journal ChemBioChem [highlighted by cover page]
Volume 2017
Number 18
Abstract The noncanonical amino acid S-allyl cysteine (Sac) is one of the major compounds of garlic extract and exhibits a range of biological activities. It is also a small bioorthogonal alkene tag capable of undergoing controlled chemical modifications, such as photoinduced thiol-ene coupling or Pd-mediated deprotection. Its small size guarantees minimal interference with protein structure and function. Here, we report a simple protocol efficiently to couple in-situ semisynthetic biosynthesis of Sac and its incorporation into proteins in response to amber (UAG) stop codons. We exploited the exceptional malleability of pyrrolysyl- tRNA synthetase (PylRS) and evolved an S-allylcysteinyltRNA synthetase (SacRS) capable of specifically accepting the small, polar amino acid instead of its long and bulky aliphatic natural substrate. We succeeded in generating a novel and inexpensive strategy for the incorporation of a functionally versatile amino acid. This will help in the conversion of orthogonal translation from a standard technique in academic research to industrial biotechnology.
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