tRNA shape is an identity element for an archaeal pyrrolysyl-tRNA synthetase from the human gut. [PDF]
Nucleic Acids Res\ua9 The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.Protein translation is orchestrated through tRNA aminoacylation and ribosomal elongation.
Krahn N +11 more
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Structure of Desulfitobacterium hafniense PylSc, a pyrrolysyl-tRNA synthetase. [PDF]
Biochem Biophys Res Commun, 2008 Pyrrolysine, the 22nd genetically-encoded amino acid, is charged onto its specific tRNA by PylS, a pyrrolysyl-tRNA synthetase. While PylS is found as a single protein in certain archaeal methanogens, in the gram-positive bacterium Desulfitobacterium hafniense, PylS is divided into two separate proteins, PylSn and PylSc, corresponding to the N-terminal ...
Lee MM +5 more
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An efficient pyrrolysyl-tRNA synthetase for economical production of MeHis-containing enzymes.
Faraday DiscussA highly efficient aminoacyl tRNA synthetase (G1PylRSMIFAF) has been developed to produce MeHis-containing proteins. High protein titres can be achieved with low ncAA concentrations (0.1 mM) enabling more economical production of MeHis-containing enzymes.
Hutton AE +7 more
europepmc +4 more sources
A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum. [PDF]
J Am Chem Soc, 2012 Together with tRNA(CUA)(Pyl), a rationally designed pyrrolysyl-tRNA synthetase mutant N346A/C348A has been successfully used for the genetic incorporation of a variety of phenylalanine derivatives with large para substituents into superfolder green fluorescent protein at an amber mutation site in Escherichia coli.
Wang YS +4 more
europepmc +4 more sources
Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool. [PDF]
Biochim Biophys Acta, 2014 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 α-amine, and low ...
Wan W, Tharp JM, Liu WR.
europepmc +4 more sources
Evolving the N-Terminal Domain of Pyrrolysyl-tRNA Synthetase for Improved Incorporation of Noncanonical Amino Acids. [PDF]
Chembiochem, 2018 AbstractBy evolving the N‐terminal domain of Methanosarcina mazei pyrrolysyl‐tRNA synthetase (PylRS) that directly interacts with tRNAPyl, a mutant clone displaying improved amber‐suppression efficiency for the genetic incorporation of Nϵ‐(tert‐butoxycarbonyl)‐l‐lysine threefold more than the wild type was identified. The identified mutations were R19H/
Sharma V +5 more
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Expanding the Scope of Orthogonal Translation with Pyrrolysyl-tRNA Synthetases Dedicated to Aromatic Amino Acids [PDF]
Molecules, 2020 In protein engineering and synthetic biology, Methanosarcina mazei pyrrolysyl-tRNA synthetase (MmPylRS), with its cognate tRNAPyl, is one of the most popular tools for site-specific incorporation of non-canonical amino acids (ncAAs).
Baumann, Tobias +5 more
core +6 more sources
Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant. [PDF]
ACS Chem Biol, 2013 When coexpressed with its cognate amber suppressing tRNACUAPyl(CUA), a pyrrolysyltRNA synthetase mutant N346A/C348A is able to genetically incorporate 12 meta-substituted phenylalanine derivatives into proteins site-specifically at amber mutation sites in Escherichia coli.
Wang YS +6 more
europepmc +4 more sources
An Expanded Toolbox for Versatile Chemical Editing of Adeno-Associated Virus. [PDF]
Angew Chem Int Ed EnglWe describe technology to introduce diverse non‐natural chemical functionalities site‐specifically into the capsid of adeno‐associated virus through genetic code expansion, and using them to engineer this leading vector for human gene therapy for enhanced tissue specificity and reduced immunogenicity Abstract Site‐specific incorporation of noncanonical
Pham Q +6 more
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Polyspecific pyrrolysyl-tRNA synthetases from directed evolution [PDF]
Proceedings of the National Academy of Sciences, 2014 Significance Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNA Pyl have emerged as ideal translation components for genetic code innovation. We found that a series of PylRS variants that were initially selected to be specific for the posttranslational modification N
Li-Tao, Guo +9 more
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