Articles with "pylrs" as a keyword



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Generating Efficient Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetases for Structurally Diverse Non-Canonical Amino Acids.

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Published in 2022 at "ACS chemical biology"

DOI: 10.1021/acschembio.2c00639

Abstract: Genetic code expansion (GCE) technologies commonly use the pyrrolysyl-tRNA synthetase (PylRS)/tRNAPyl pairs from Methanosarcina mazei (Mm) and Methanosarcina barkeri (Mb) for site-specific incorporation of non-canonical amino acids (ncAAs) into proteins. Recently a homologous PylRS/tRNAPyl pair… read more here.

Keywords: pylrs; non canonical; canonical amino; pyrrolysyl trna ... See more keywords
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Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase

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Published in 2017 at "Nature chemical biology"

DOI: 10.1038/nchembio.2497

Abstract: Pyrrolysyl-tRNA synthetase (PylRS) is a major tool in genetic code expansion with non-canonical amino acids, yet understanding of its structure and activity is incomplete. Here we describe the crystal structure of the previously uncharacterized essential… read more here.

Keywords: pyrrolysyl trna; pylrs; trna synthetase; structure ... See more keywords
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Update of the Pyrrolysyl-tRNA Synthetase/tRNAPyl Pair and Derivatives for Genetic Code Expansion

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Published in 2023 at "Journal of Bacteriology"

DOI: 10.1128/jb.00385-22

Abstract: The cotranslational incorporation of pyrrolysine (Pyl), the 22nd proteinogenic amino acid, into proteins in response to the UAG stop codon represents an outstanding example of natural genetic code expansion. Genetic encoding of Pyl is conducted… read more here.

Keywords: genetic code; code expansion; trnapyl; pylrs ... See more keywords
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Linker and N-Terminal Domain Engineering of Pyrrolysyl-tRNA Synthetase for Substrate Range Shifting and Activity Enhancement

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Published in 2020 at "Frontiers in Bioengineering and Biotechnology"

DOI: 10.3389/fbioe.2020.00235

Abstract: The Methanosarcina mazei pyrrolysyl-tRNA synthetase (PylRS)â‹…tRNAPyl pair can be used to incorporate non-canonical amino acids (ncAAs) into proteins at installed amber stop codons. Although engineering of the PylRS active site generates diverse binding pockets, the… read more here.

Keywords: pyrrolysyl trna; pylrs; linker; domain ... See more keywords