scholarly journals Coding triplets in the tRNA acceptor‐TΨC arm and their role in present and past tRNA recognition

FEBS Letters ◽  
2021 ◽  
Author(s):  
Ilana Agmon ◽  
Itay Fayerverker ◽  
Tal Mor
2019 ◽  
Author(s):  
Ilana Agmon ◽  
Itay Fayerverker ◽  
Tal Mor

AbstractThe mechanism and evolution of the recognition scheme between key components of the translation system, i.e., tRNAs, synthetases and elongation factors, are fundamental issues in understanding the translation of genetic information into proteins. Statistical analysis of bacterial tRNA sequences reveals that for six amino acids, i.e. for Ala, Asp, Gly, His, Pro and Ser, a string of 10 nucleotides preceding the tRNA 3’end, carries cognate coding triplets to nearly full extent. The triplets conserved in positions 63-67 are implicated in the recognition by EF-Tu, and those conserved in positions 68-72, in the identification of cognate tRNAs and their derived minihelices, by class IIa synthetases. These coding triplets are suggested to have primordial origin, being engaged in aminoacylation of prebiotic tRNAs and in the establishment of the canonical codon set.


Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15322-15331 ◽  
Author(s):  
Fabrice Agou ◽  
Sophie Quevillon ◽  
Pierre Kerjan ◽  
Marie-Thérèse Latreille ◽  
Marc Mirande

Biochemistry ◽  
1997 ◽  
Vol 36 (26) ◽  
pp. 7967-7972 ◽  
Author(s):  
Christian S. Hamann ◽  
Ya-Ming Hou

2009 ◽  
Vol 38 (2) ◽  
pp. 672-682 ◽  
Author(s):  
Akiyoshi Nakamura ◽  
Kelly Sheppard ◽  
Junji Yamane ◽  
Min Yao ◽  
Dieter Söll ◽  
...  

2019 ◽  
Vol 47 (6) ◽  
pp. 3072-3085 ◽  
Author(s):  
Qi-Yu Zeng ◽  
Gui-Xin Peng ◽  
Guang Li ◽  
Jing-Bo Zhou ◽  
Wen-Qiang Zheng ◽  
...  

2020 ◽  
Vol 48 (6) ◽  
pp. 3181-3194 ◽  
Author(s):  
Jing-Bo Zhou ◽  
Yong Wang ◽  
Qi-Yu Zeng ◽  
Shi-Xin Meng ◽  
En-Duo Wang ◽  
...  

Abstract N 6-Threonylcarbamoyladenosine (t6A) is a universal tRNA modification essential for translational accuracy and fidelity. In human mitochondria, YrdC synthesises an l-threonylcarbamoyl adenylate (TC-AMP) intermediate, and OSGEPL1 transfers the TC-moiety to five tRNAs, including human mitochondrial tRNAThr (hmtRNAThr). Mutation of hmtRNAs, YrdC and OSGEPL1, affecting efficient t6A modification, has been implicated in various human diseases. However, little is known about the tRNA recognition mechanism in t6A formation in human mitochondria. Herein, we showed that OSGEPL1 is a monomer and is unique in utilising C34 as an anti-determinant by studying the contributions of individual bases in the anticodon loop of hmtRNAThr to t6A modification. OSGEPL1 activity was greatly enhanced by introducing G38A in hmtRNAIle or the A28:U42 base pair in a chimeric tRNA containing the anticodon stem of hmtRNASer(AGY), suggesting that sequences of specific hmtRNAs are fine-tuned for different modification levels. Moreover, using purified OSGEPL1, we identified multiple acetylation sites, and OSGEPL1 activity was readily affected by acetylation via multiple mechanisms in vitro and in vivo. Collectively, we systematically elucidated the nucleotide requirement in the anticodon loop of hmtRNAs, and revealed mechanisms involving tRNA sequence optimisation and post-translational protein modification that determine t6A modification levels.


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