scholarly journals Binding and recognition of aminoacyl-tRNA synthetase by cognate tRNA

1973 ◽  
Vol 13 (4) ◽  
pp. 172-186
Author(s):  
Takeshi SENO
Keyword(s):  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Cognate Trna

scholarly journals The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

2021 ◽  
Author(s):  
Gabor L. Igloi
Keyword(s):  
Protein Sequence ◽  
Identity Element ◽  
Mitochondrial Gene ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Cognate Trna ◽  
Evolutionary Fate ◽  
Endosymbiotic Evolution

AbstractDuring the endosymbiotic evolution of mitochondria, the genes for aminoacyl-tRNA synthetases were transferred to the ancestral nucleus. A further reduction of mitochondrial function resulted in mitochondrion-related organisms (MRO) with a loss of the organelle genome. The fate of the now redundant ancestral mitochondrial aminoacyl-tRNA synthetase genes is uncertain. The derived protein sequence for arginyl-tRNA synthetase from thirty mitosomal organisms have been classified as originating from the ancestral nuclear or mitochondrial gene and compared to the identity element at position 20 of the cognate tRNA that distinguishes the two enzyme forms. The evolutionary choice between loss and retention of the ancestral mitochondrial gene for arginyl-tRNA synthetase reflects the coevolution of arginyl-tRNA synthetase and tRNA identity elements.

scholarly journals Directed-evolution of translation system for efficient unnatural amino acids incorporation and generalizable synthetic auxotroph construction

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Hongxia Zhao ◽  
Wenlong Ding ◽  
Jia Zang ◽  
Yang Yang ◽  
Chao Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Background Activity ◽  
Trna Synthetase ◽  
Translation System ◽  
Aminoacyl Trna Synthetase ◽  
E Coli ◽  
Natural Amino Acids ◽  
Translation Systems ◽  
Cognate Trna

AbstractSite-specific incorporation of unnatural amino acids (UAAs) with similar incorporation efficiency to that of natural amino acids (NAAs) and low background activity is extremely valuable for efficient synthesis of proteins with diverse new chemical functions and design of various synthetic auxotrophs. However, such efficient translation systems remain largely unknown in the literature. Here, we describe engineered chimeric phenylalanine systems that dramatically increase the yield of proteins bearing UAAs, through systematic engineering of the aminoacyl-tRNA synthetase and its respective cognate tRNA. These engineered synthetase/tRNA pairs allow single-site and multi-site incorporation of UAAs with efficiencies similar to those of NAAs and high fidelity. In addition, using the evolved chimeric phenylalanine system, we construct a series of E. coli strains whose growth is strictly dependent on exogenously supplied of UAAs. We further show that synthetic auxotrophic cells can grow robustly in living mice when UAAs are supplemented.

Analysis of the aminoacyl-tRNA synthetase genes of silkworm (Bombyx mori)

2009 ◽  
Vol 31 (12) ◽  
pp. 1248-1258
Author(s):  
Guang-Li CAO ◽  
Ren-Yu XUE ◽  
Yue-Xiong ZHU ◽  
Yu-Hong WEI ◽  
Cheng-Liang GONG
Keyword(s):  
Bombyx Mori ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase

Directed evolution of an improved aminoacyl‐tRNA synthetase for incorporation of L‐3,4‐dihydroxyphenylalanine (L‐DOPA)

2021 ◽  
Author(s):  
Ross Thyer ◽  
Simon d’Oelsnitz ◽  
Molly S. Blevins ◽  
Dustin R. Klein ◽  
Jennifer S. Brodbelt ◽  
...  
Keyword(s):  
Directed Evolution ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase
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