Professor Wang Chien-Chia's Team Discovered Key Evidence for the Evolution of an Enzyme Used in Translation. The Research Was Published in Nucleic Acids Research.

Professor Wang Chien-Chia and Indonesian doctoral student Titi Rindi Antika in the Department of Life Sciences at National Central University have dedicated themselves to decoding genetic information and successfully discovered key evidence for the evolution of the translation enzyme aminoacyl-tRNA synthetase (aaRS). The result was published in Nucleic Acids Research, a leading international journal with an impact factor of 16.971. This research result has not only taken the translation of the genetic code one step forward but also benefited the treatment of relevant diseases. Professor Wang’s team has unexpectedly discovered that Caenorhabditis elegans’s alanyl-tRNA synthetase (AlaRS) is different from its mitochondrial counterpart. The tail end of the synthetase lacks a functional domain; also, the three-dimensional structure of its cognate tRNA is not L-shaped. This distinctive difference encouraged them to do further research on the role of the synthetase in this functional domain. After repeated analyses, experiments, and verifications, they finally confirmed that the functional domain is used to identify and bind tRNA. The binding site happens to locate at the corner of the L-shaped tRNAAla. Therefore, without this functional domain, the synthetase cannot effectively identify and bind the L-shaped modern tRNA. Professor Wang's team has dedicated themselves to tRNA research for 20 years, focusing mainly on the analysis of the molecular mechanism of gene decoding and its correlation with diseases. The key enzyme—aminoacyl-tRNA synthetase (aaRS)—is not only involved in protein synthesis but also closely related to cancer development, vascular regeneration, immunity, neurodevelopment, etc. Using synthetases as targets, we can develop a new generation of antibiotics to fight against the increasingly rampant "superbugs."