Pyrrolysyl-tRNA synthetase: An ordinary enzyme but an outstanding genetic code expansion tool Academic Article uri icon

abstract

  • The genetic incorporation of the 22nd proteinogenic amino acid, pyrrolysine (Pyl) at amber codon is achieved by the action of pyrrolysyl-tRNA synthetase (PylRS) together with its cognate tRNAPyl. Unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate -amine, and low selectivity toward the anticodon of tRNAPyl. These unique but ordinary features of PylRS as an aminoacyl-tRNA synthetase allow the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (NCAAs) or -hydroxy acids into proteins at amber codon and the reassignment of other codons such as ochre UAA, opal UGA, and four-base AGGA codons to code NCAAs. 2014 Elsevier B.V.

published proceedings

  • Biochimica et Biophysica Acta - Proteins and Proteomics

altmetric score

  • 28.884

author list (cited authors)

  • Wan, W., Tharp, J. M., & Liu, W. R.

citation count

  • 277

complete list of authors

  • Wan, W||Tharp, JM||Liu, WR

publication date

  • January 2014