Engineering Pyrrolysyl-tRNA Synthetase for the Incorporation of Non-Canonical Amino Acids with Smaller Side Chains. [PDF]
Int J Mol Sci, 2021 Site-specific incorporation of non-canonical amino acids (ncAAs) into proteins has emerged as a universal tool for systems bioengineering at the interface of chemistry, biology, and technology.
Koch NG +3 more
europepmc +9 more sources
Efficient Unnatural Protein Production by Pyrrolysyl-tRNA Synthetase With Genetically Fused Solubility Tags. [PDF]
Front Bioeng Biotechnol, 2021 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.
Koch NG, Baumann T, Budisa N.
europepmc +8 more sources
Quintuply orthogonal pyrrolysyl-tRNA synthetase/tRNAPyl pairs. [PDF]
Nat Chem, 2023 Mutually orthogonal aminoacyl transfer RNA synthetase/transfer RNA pairs provide a foundation for encoding non-canonical amino acids into proteins, and encoded non-canonical polymer and macrocycle synthesis. Here we discover quintuply orthogonal pyrrolysyl-tRNA synthetase (PylRS)/pyrrolysyl-tRNA (tRNAPyl) pairs.
Beattie AT, Dunkelmann DL, Chin JW.
europepmc +4 more sources
Exploration of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Activity in Yeast. [PDF]
ACS Synth Biol, 2022 AbstractArchaeal pyrrolysyl-tRNA synthetases (PylRSs) have been used to genetically encode over 200 distinct noncanonical amino acids (ncAAs) in proteins in E. coli and mammalian cells. This vastly expands the range of chemical functionality accessible within proteins produced in these organisms.
Stieglitz JT +3 more
europepmc +4 more sources
Enhancing the performance of a mutant pyrrolysyl-tRNA synthetase to create a highly versatile eukaryotic cell-free protein synthesis tool. [PDF]
Sci Rep, 2023 Modification of proteins with a broad range of chemical functionalities enables the investigation of protein structure and activity by manipulating polypeptides at single amino acid resolution.
Schloßhauer JL +5 more
europepmc +3 more sources
Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs. [PDF]
Nat Chem, 2018 Genetically encoding distinct non-canonical amino acids (ncAAs) into proteins synthesized in cells requires mutually orthogonal aminoacyl-tRNA synthetase (aaRS)/tRNA pairs. The pyrrolysyl-tRNA synthetase/PyltRNA pair from Methanosarcina mazei (Mm) has been engineered to incorporate diverse ncAAs and is commonly considered an ideal pair for genetic code
Willis JCW, Chin JW.
europepmc +4 more sources
Genetic Incorporation of ϵ-N-Benzoyllysine by Engineering Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase. [PDF]
Chembiochem, 2021 AbstractPost‐translational modifications regulate protein structure and function. Lysine benzoylation is a newly discovered histone modification with unique physiological relevance. To construct proteins with this modification site‐specifically, we generated orthogonal tRNAPyl‐MaBzKRS pairs by engineering Methanomethylophilus alvus pyrrolysyl‐tRNA ...
Cao L +4 more
europepmc +5 more sources
Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion. [PDF]
Chem RevChemical Reviews, 124 (16)
Koch NG, Budisa N.
europepmc +4 more sources
Directed Evolution of Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase Generates a Hyperactive and Highly Selective Variant. [PDF]
Front Mol Biosci, 2022 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 the incorporation of difficult ncAAs.
Fischer JT, Söll D, Tharp JM.
europepmc +4 more sources
Pyrrolysyl-tRNA-Synthetase: Methanogenese und Gencode-Erweiterung [PDF]
BIOspektrum, 2021 Pyrrolysyl-tRNA synthetase (PylRS) is an enzyme of some methanogenic Archaea for the natural incorporation of pyrrolysine into proteins. The discovery of PylRS as a natural tool for genetic code expansion paved the way for site-specific incorporation of ...
Budisa, Nediljko, Koch, Nikolaj Georg
core +4 more sources