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

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)2190-2200
Number of pages11
JournalNucleic Acids Research
Volume50
Issue number4
DOIs
StatePublished - 28 Feb 2022

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