Articles with "pyrrolysyl trna" 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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Exploration of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Activity in Yeast.

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Published in 2022 at "ACS synthetic biology"

DOI: 10.1021/acssynbio.2c00001

Abstract: Archaeal pyrrolysyl-tRNA synthetases (PylRSs) have been used to genetically encode over 200 distinct noncanonical amino acids (ncAAs) in proteins in Escherichia coli and mammalian cells. This vastly expands the range of chemical functionality accessible within… read more here.

Keywords: methanomethylophilus alvus; activity; yeast; 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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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
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Efficient Unnatural Protein Production by Pyrrolysyl-tRNA Synthetase With Genetically Fused Solubility Tags

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Published in 2021 at "Frontiers in Bioengineering and Biotechnology"

DOI: 10.3389/fbioe.2021.807438

Abstract: Introducing non-canonical amino acids (ncAAs) by engineered orthogonal pairs of aminoacyl-tRNA synthetases and tRNAs has proven to be a highly useful tool for the expansion of the genetic code. Pyrrolysyl-tRNA synthetase (PylRS) from methanogenic archaeal… read more here.

Keywords: pyrrolysyl trna; production; protein; solubility ... See more keywords

Directed Evolution of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Generates a Hyperactive and Highly Selective Variant

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Published in 2022 at "Frontiers in Molecular Biosciences"

DOI: 10.3389/fmolb.2022.850613

Abstract: Pyrrolysyl-tRNA synthetase (PylRS) is frequently used for site-specific incorporation of noncanonical amino acids (ncAAs) into proteins. Recently, the active site of Methanomethylophilus alvus PylRS (MaPylRS) has been rationally engineered to expand its substrate compatibility, enabling… read more here.

Keywords: trna synthetase; pyrrolysyl trna; methanomethylophilus alvus; directed evolution ... See more keywords
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Rapid Identification of Functional Pyrrolysyl-tRNA Synthetases via Fluorescence-Activated Cell Sorting

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Published in 2018 at "International Journal of Molecular Sciences"

DOI: 10.3390/ijms20010029

Abstract: The orthogonal pyrrolysyl-tRNA synthetase/tRNACUA pair and their variants have provided powerful tools for expanding the genetic code to allow for engineering of proteins with augmented structure and function not present in Nature. To expedite the… read more here.

Keywords: pyrrolysyl trna; pyrrolysyl; activated cell; cell sorting ... See more keywords