Covariation of a Specificity-Determining Structural Motif in an Aminoacyl-tRNA Synthetase and a tRNA Identity Element†

Biochemistry ◽  
2001 ◽  
Vol 40 (7) ◽  
pp. 1930-1936 ◽  
Author(s):  
Susan A. Hawko ◽  
Christopher S. Francklyn
Keyword(s):  
Identity Element ◽  
Trna Synthetase ◽  
Structural Motif ◽  
Aminoacyl Trna Synthetase

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 A Temporal Order in 5′- and 3′- Processing of Eukaryotic tRNAHis

2019 ◽  
Vol 20 (6) ◽  
pp. 1384 ◽  
Author(s):  
Marie-Theres Pöhler ◽  
Tracy Roach ◽  
Heike Betat ◽  
Jane Jackman ◽  
Mario Mörl
Keyword(s):  
Temporal Order ◽  
Unique Feature ◽  
Identity Element ◽  
Random Order ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Substrate Preferences ◽  
Positive Elements ◽  
Trna Species ◽  
Important Processing

For flawless translation of mRNA sequence into protein, tRNAs must undergo a series of essential maturation steps to be properly recognized and aminoacylated by aminoacyl-tRNA synthetase, and subsequently utilized by the ribosome. While all tRNAs carry a 3′-terminal CCA sequence that includes the site of aminoacylation, the additional 5′-G-1 position is a unique feature of most histidine tRNA species, serving as an identity element for the corresponding synthetase. In eukaryotes including yeast, both 3′-CCA and 5′-G-1 are added post-transcriptionally by tRNA nucleotidyltransferase and tRNAHis guanylyltransferase, respectively. Hence, it is possible that these two cytosolic enzymes compete for the same tRNA. Here, we investigate substrate preferences associated with CCA and G-1-addition to yeast cytosolic tRNAHis, which might result in a temporal order to these important processing events. We show that tRNA nucleotidyltransferase accepts tRNAHis transcripts independent of the presence of G-1; however, tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. Although many tRNA maturation steps can occur in a rather random order, our data demonstrate a likely pathway where CCA-addition precedes G-1 incorporation in S. cerevisiae. Evidently, the 3′-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition.

Role for a Conserved Structural Motif in Assembly of a Class I Aminoacyl-tRNA Synthetase Active Site

Biochemistry ◽  
2011 ◽  
Vol 50 (5) ◽  
pp. 763-769 ◽  
Author(s):  
Veronica C. Casina ◽  
Andrew A. Lobashevsky ◽  
William E. McKinney ◽  
Cassidy L. Brown ◽  
Rebecca W. Alexander
Keyword(s):  
Active Site ◽  
Trna Synthetase ◽  
Class I ◽  
Structural Motif ◽  
Aminoacyl Trna Synthetase

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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