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The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity [PDF]
FEBS Letters, 2007 Pyrrolysine (Pyl) is co-translationally inserted into a subset of proteins in the Methanosarcinaceae and in Desulfitobacterium hafniense programmed by an in-frame UAG stop codon. Suppression of this UAG codon is mediated by the Pyl amber suppressor tRNA,
Carla Polycarpo +2 more
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Engineering a Polyspecific Pyrrolysyl-tRNA Synthetase by a High Throughput FACS Screen
Scientific Reports, 2019 The Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNAPyl are extensively used to add non-canonical amino acids (ncAAs) to the genetic code of bacterial and eukaryotic cells.
Adrian Hohl +2 more
exaly +2 more sources
ACS Chemical Biology, 2018 Genetic code expansion via stop codon suppression is a versatile tool for engineering proteins in mammalian cells with site-specifically encoded non-canonical amino acids (ncAAs).
Lorenzo Lafranchi +2 more
exaly +2 more sources
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Optimization of genetic code expansion in the baculovirus expression vector system (BEVS)
Protein Expression and Purification, 2023Ciarán N Cronin
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Quintuply orthogonal pyrrolysyl-tRNA synthetase/tRNAPyl pairs
Nature Chemistry, 2023Daniel Dunkelmann +2 more
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Pyrrolysine analogues as substrates for pyrrolysyl-tRNA synthetase
FEBS Letters, 2006Carla Polycarpo +2 more
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Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs
Nature Chemistry, 2018Julian C W Willis, Jason W. Chin
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