Gain of C-Ala enables AlaRS to target the L-shaped tRNAAla

Titi Rindi Antika, Dea Jolie Chrestella, Indira Rizqita Ivanesthi, Gita Riswana Nawung Rida, Kuan Yu Chen, Fu Guo Liu, Yi Chung Lee, Yu Wei Chen, Yi Kuan Tseng, Chien Chia Wang

研究成果: 雜誌貢獻期刊論文同行評審

5 引文 斯高帕斯(Scopus)


Unlike many other aminoacyl-tRNA synthetases, alanyl-tRNA synthetase (AlaRS) retains a conserved prototype structure throughout biology. While Caenorhabditis elegans cytoplasmic AlaRS (CeAlaRSc) retains the prototype structure, its mitochondrial counterpart (CeAlaRSm) contains only a residual C-terminal domain (C-Ala). We demonstrated herein that the C-Ala domain from CeAlaRSc robustly binds both tRNA and DNA. It bound different tRNAs but preferred tRNAAla. Deletion of this domain from CeAlaRSc sharply reduced its aminoacylation activity, while fusion of this domain to CeAlaRSm selectively and distinctly enhanced its aminoacylation activity toward the elbow-containing (or L-shaped) tRNAAla. Phylogenetic analysis showed that CeAlaRSm once possessed the C-Ala domain but later lost most of it during evolution, perhaps in response to the deletion of the T-arm (part of the elbow) from its cognate tRNA. This study underscores the evolutionary gain of C-Ala for docking AlaRS to the L-shaped tRNAAla.

頁(從 - 到)2190-2200
期刊Nucleic Acids Research
出版狀態已出版 - 28 2月 2022


深入研究「Gain of C-Ala enables AlaRS to target the L-shaped tRNAAla」主題。共同形成了獨特的指紋。