Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1844, Issue 6, Pages 1059-1070Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2014.03.002
Keywords
Pyrrolysine; Amber codon; Genetic code expansion; Non-canonical amino acids; Hydroxy acids
Categories
Funding
- National Institutes of Health [1R01CA161158]
- National Science Foundation [CHEM-1148684]
- Welch Foundation [A-1715]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1148684] Funding Source: National Science Foundation
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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 tRNA(Pyl). Unlike most aminoacyl-tRNA synthetases, PylRS displays high substrate side chain promiscuity, low selectivity toward its substrate et-amine, and low selectivity toward the anticodon of tRNA(Pyl). 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 alpha-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. (C) 2014 Elsevier B.V. All rights reserved.
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