Synthesis of Threefold Glycosylated Proteins using Click Chemistry and Genetically Encoded Unnatural Amino Acids

ChemBioChem ◽  
2009 ◽  
Vol 10 (18) ◽  
pp. 2858-2861 ◽  
Author(s):  
Emine Kaya ◽  
Katrin Gutsmiedl ◽  
Milan Vrabel ◽  
Markus Müller ◽  
Peter Thumbs ◽  
...  
Keyword(s):  
Amino Acids ◽  
Click Chemistry ◽  
Unnatural Amino Acids ◽  
Glycosylated Proteins

scholarly journals Combined Use of Unnatural Amino Acids Enables Dual-Color Super-Resolution Imaging of Proteins via Click Chemistry

ACS Nano ◽  
2018 ◽  
Vol 12 (12) ◽  
pp. 12247-12254 ◽  
Author(s):  
Kim-A. Saal ◽  
Frank Richter ◽  
Peter Rehling ◽  
Silvio O. Rizzoli
Keyword(s):  
Amino Acids ◽  
Click Chemistry ◽  
Unnatural Amino Acids ◽  
Super Resolution ◽  
Dual Color ◽  
Combined Use ◽  
Resolution Imaging

scholarly journals Enzymatic aminoacylation of tRNA with unnatural amino acids

2006 ◽  
Vol 103 (12) ◽  
pp. 4356-4361 ◽  
Author(s):  
M. C. T. Hartman ◽  
K. Josephson ◽  
J. W. Szostak
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids

scholarly journals Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency

Amino Acids ◽  
2020 ◽  
Author(s):  
Thomas L. Williams ◽  
Debra J. Iskandar ◽  
Alexander R. Nödling ◽  
Yurong Tan ◽  
Louis Y. P. Luk ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Genetic Code ◽  
Unnatural Amino Acids ◽  
Trna Synthetase ◽  
Unnatural Amino Acid ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Genetic Code Expansion ◽  
Incorporation Efficiency

AbstractGenetic code expansion is a powerful technique for site-specific incorporation of an unnatural amino acid into a protein of interest. This technique relies on an orthogonal aminoacyl-tRNA synthetase/tRNA pair and has enabled incorporation of over 100 different unnatural amino acids into ribosomally synthesized proteins in cells. Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNA from Methanosarcina species are arguably the most widely used orthogonal pair. Here, we investigated whether beneficial effect in unnatural amino acid incorporation caused by N-terminal mutations in PylRS of one species is transferable to PylRS of another species. It was shown that conserved mutations on the N-terminal domain of MmPylRS improved the unnatural amino acid incorporation efficiency up to five folds. As MbPylRS shares high sequence identity to MmPylRS, and the two homologs are often used interchangeably, we examined incorporation of five unnatural amino acids by four MbPylRS variants at two temperatures. Our results indicate that the beneficial N-terminal mutations in MmPylRS did not improve unnatural amino acid incorporation efficiency by MbPylRS. Knowledge from this work contributes to our understanding of PylRS homologs which are needed to improve the technique of genetic code expansion in the future.

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