Sequence-specific targeting of Caenorhabditis elegans C-Ala to the D-loop of tRNAAla

Titi Rindi Antika, Kun Rohmatan Nazilah, Dea Jolie Chrestella, Tzu Ling Wang, Yi Kuan Tseng, Sun Chong Wang, Hsin Ling Hsu, Shao Win Wang, Tsung Hsien Chuang, Hung Chuan Pan, Jia Cherng Horng, Chien Chia Wang

Research output: Contribution to journalArticlepeer-review


Alanyl-tRNA synthetase retains a conserved prototype structure throughout its biology. Nevertheless, its C-terminal domain (C-Ala) is highly diverged and has been shown to play a role in either tRNA or DNA binding. Interestingly, we discovered that Caenorhabditis elegans cytoplasmic C-Ala (Ce-C-Alac) robustly binds both ligands. How Ce-C-Alac targets its cognate tRNA and whether a similar feature is conserved in its mitochondrial counterpart remain elusive. We show that the N- and C-terminal subdomains of Ce-C-Alac are responsible for DNA and tRNA binding, respectively. Ce-C-Alac specifically recognized the conserved invariant base G18 in the D-loop of tRNAAla through a highly conserved lysine residue, K934. Despite bearing little resemblance to other C-Ala domains, C. elegans mitochondrial C-Ala robustly bound both tRNAAla and DNA and maintained targeting specificity for the D-loop of its cognate tRNA. This study uncovers the underlying mechanism of how C. elegans C-Ala specifically targets the D-loop of tRNAAla.

Original languageEnglish
Article number105149
JournalJournal of Biological Chemistry
Issue number9
StatePublished - Sep 2023


  • Caenorhabditis elegans
  • DNA-binding domain
  • aminoacyl-tRNA synthetase
  • coevolution
  • tRNA-binding domain
  • translation


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