Ontology highlight
ABSTRACT:
SUBMITTER: Antika TR
PROVIDER: S-EPMC10485164 | biostudies-literature | 2023 Aug
REPOSITORIES: biostudies-literature
Antika Titi Rindi TR Nazilah Kun Rohmatan KR Chrestella Dea Jolie DJ Wang Tzu-Ling TL Tseng Yi-Kuan YK Wang Sun-Chong SC Hsu Hsin-Ling HL Wang Shao-Win SW Chuang Tsung-Hsien TH Pan Hung-Chuan HC Horng Jia-Cherng JC Wang Chien-Chia CC
The Journal of biological chemistry 20230809 9
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-Ala<sub>c</sub>) robustly binds both ligands. How Ce-C-Ala<sub>c</sub> targets its cognate tRNA and whether a similar feature is conserved in its mitochondrial counterpart remain elusive. We show that the ...[more]