scholarly journals Inhibition of Arabidopsis growth by the allelopathic compound azetidine-2-carboxylate is due to the low amino acid specificity of cytosolic prolyl-tRNA synthetase

2016 ◽  
Vol 88 (2) ◽  
pp. 236-246 ◽  
Author(s):  
Jiyeon Lee ◽  
Naveen Joshi ◽  
Rita Pasini ◽  
Renwick C. J. Dobson ◽  
Jane Allison ◽  
...  
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Allelopathic Compound

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.

Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase

DNA Sequence ◽  
1994 ◽  
Vol 4 (4) ◽  
pp. 243-248 ◽  
Author(s):  
Matt E. Cruzen ◽  
Stuart M. Arfin
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trna Synthetase

Structural Basis of Furan-Amino Acid Recognition by a Polyspecific Aminoacyl-tRNA-Synthetase and its Genetic Encoding in Human Cells

ChemBioChem ◽  
2014 ◽  
Vol 15 (12) ◽  
pp. 1755-1760 ◽  
Author(s):  
Moritz J. Schmidt ◽  
Annemarie Weber ◽  
Moritz Pott ◽  
Wolfram Welte ◽  
Daniel Summerer
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Human Cells ◽  
Structural Basis ◽  
Aminoacyl Trna Synthetase ◽  
Genetic Encoding ◽  
Amino Acid Recognition

Functional Replacement of Hamster Lysyl-tRNA Synthetase by the Yeast Enzyme Requires Cognate Amino Acid Sequences for Proper tRNA Recognition†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15322-15331 ◽  
Author(s):  
Fabrice Agou ◽  
Sophie Quevillon ◽  
Pierre Kerjan ◽  
Marie-Thérèse Latreille ◽  
Marc Mirande
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Sequences ◽  
Trna Recognition ◽  
Functional Replacement

scholarly journals A Unique Insert of Leucyl-tRNA Synthetase Is Required for Aminoacylation and Not Amino Acid Editing†

Biochemistry ◽  
2007 ◽  
Vol 46 (17) ◽  
pp. 5170-5176 ◽  
Author(s):  
Michael T. Vu ◽  
Susan A. Martinis
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Editing

Nucleotide Determinants for tRNA-Dependent Amino Acid Discrimination by a Class I tRNA Synthetase†

Biochemistry ◽  
1999 ◽  
Vol 38 (51) ◽  
pp. 16898-16903 ◽  
Author(s):  
Mark A. Farrow ◽  
Brian E. Nordin ◽  
Paul Schimmel
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Class I

scholarly journals Amino Acid Residues Required for Maturation, Cell Uptake, and Processing of Translation Inhibitor Microcin C

2006 ◽  
Vol 189 (5) ◽  
pp. 2114-2118 ◽  
Author(s):  
Teymur Kazakov ◽  
Anastasia Metlitskaya ◽  
Konstantin Severinov
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Trojan Horse ◽  
Cell Uptake ◽  
Amino Acid Residues ◽  
Peptide Moiety ◽  
Translation Inhibitor ◽  
Mutational Study ◽  
The Way

ABSTRACT Microcin C (McC), a peptide-nucleotide Trojan horse antibiotic, targets aspartyl-tRNA synthetase. We present the results of a systematic mutational study of the 7-amino-acid ribosomally synthesized peptide moiety of McC. Our results define amino acid positions important for McC maturation and cell uptake and processing and open the way for creation of more potent McC-based inhibitors.

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