scholarly journals Isolated CP1 Domain ofEscherichia coliLeucyl-tRNA Synthetase Is Dependent on Flanking Hinge Motifs for Amino Acid Editing Activity†

Biochemistry ◽  
2007 ◽  
Vol 46 (21) ◽  
pp. 6258-6267 ◽  
Author(s):  
Aswini K. Betha ◽  
Amy M. Williams ◽  
Susan A. Martinis
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Editing ◽  
Editing Activity

scholarly journals A Viable Amino Acid Editing Activity in the Leucyl-tRNA Synthetase CP1-splicing Domain Is Not Required in the Yeast Mitochondria

2006 ◽  
Vol 281 (44) ◽  
pp. 33217-33225 ◽  
Author(s):  
Vrajesh A. Karkhanis ◽  
Michal T. Boniecki ◽  
Kiranmai Poruri ◽  
Susan A. Martinis
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Yeast Mitochondria ◽  
Amino Acid Editing ◽  
Editing Activity

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

Rational Design to Block Amino Acid Editing of a tRNA Synthetase

2002 ◽  
Vol 124 (25) ◽  
pp. 7286-7287 ◽  
Author(s):  
Richard S. Mursinna ◽  
Susan A. Martinis
Keyword(s):  
Amino Acid ◽  
Rational Design ◽  
Trna Synthetase ◽  
Amino Acid Editing

scholarly journals Amino Acid Toxicities of Escherichia coli That Are Prevented by Leucyl-tRNA Synthetase Amino Acid Editing

2007 ◽  
Vol 189 (23) ◽  
pp. 8765-8768 ◽  
Author(s):  
Vrajesh A. Karkhanis ◽  
Anjali P. Mascarenhas ◽  
Susan A. Martinis
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Editing

ABSTRACT Leucyl-tRNA synthetase (LeuRS) has evolved an editing function to clear misactivated amino acids. An Escherichia coli-based assay was established to identify amino acids that compromise the fidelity of LeuRS and translation. Multiple nonstandard as well as standard amino acids were toxic to the cell when LeuRS editing was inactivated.

scholarly journals Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase

2006 ◽  
Vol 103 (40) ◽  
pp. 14744-14749 ◽  
Author(s):  
H. M. Sasaki ◽  
S.-i. Sekine ◽  
T. Sengoku ◽  
R. Fukunaga ◽  
M. Hattori ◽  
...  
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Editing ◽  
Editing Domain

scholarly journals Cross-editing by a tRNA synthetase allows vertebrates to abundantly express mischargeable tRNA without causing mistranslation

2020 ◽  
Vol 48 (12) ◽  
pp. 6445-6457 ◽  
Author(s):  
Meirong Chen ◽  
Bernhard Kuhle ◽  
Jolene Diedrich ◽  
Ze Liu ◽  
James J Moresco ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Mammalian Cells ◽  
Trna Synthetase ◽  
Intrinsic Activity ◽  
Trna Synthetases ◽  
Evolutionarily Conserved ◽  
Trna Species ◽  
In Trans ◽  
Editing Activity

Abstract The accuracy in pairing tRNAs with correct amino acids by aminoacyl-tRNA synthetases (aaRSs) dictates the fidelity of translation. To ensure fidelity, multiple aaRSs developed editing functions that remove a wrong amino acid from tRNA before it reaches the ribosome. However, no specific mechanism within an aaRS is known to handle the scenario where a cognate amino acid is mischarged onto a wrong tRNA, as exemplified by AlaRS mischarging alanine to G4:U69-containing tRNAThr. Here, we report that the mischargeable G4:U69-containing tRNAThr are strictly conserved in vertebrates and are ubiquitously and abundantly expressed in mammalian cells and tissues. Although these tRNAs are efficiently mischarged, no corresponding Thr-to-Ala mistranslation is detectable. Mistranslation is prevented by a robust proofreading activity of ThrRS towards Ala-tRNAThr. Therefore, while wrong amino acids are corrected within an aaRS, a wrong tRNA is handled in trans by an aaRS cognate to the mischarged tRNA species. Interestingly, although Ala-tRNAThr mischarging is not known to occur in bacteria, Escherichia coli ThrRS also possesses robust cross-editing ability. We propose that the cross-editing activity of ThrRS is evolutionarily conserved and that this intrinsic activity allows G4:U69-containing tRNAThr to emerge and be preserved in vertebrates to have alternative functions without compromising translational fidelity.

scholarly journals A Paradigm Shift for the Amino Acid Editing Mechanism of Human Cytoplasmic Leucyl-tRNA Synthetase

Biochemistry ◽  
2009 ◽  
Vol 48 (38) ◽  
pp. 8958-8964 ◽  
Author(s):  
Yan Ling Joy Pang ◽  
Susan A. Martinis
Keyword(s):  
Amino Acid ◽  
Paradigm Shift ◽  
Trna Synthetase ◽  
Amino Acid Editing
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