A metal ion mediated functional dichotomy encodes plasticity during translation quality control.

ABSTRACT: Proofreading during translation of the genetic code is a key process for not only translation quality control but also for its modulation under stress conditions to provide fitness advantage. A major class of proofreading modules represented by editing domains of alanyl-tRNA synthetase (AlaRS-Ed) and threonyl-tRNA synthetase (ThrRS-Ed) features a common fold and an invariant Zn²⁺ binding motif across life forms. Here, we reveal the structural basis and functional consequence along with the necessity for their operational dichotomy, i.e., the metal ion is ubiquitous in one and inhibitor for the other. The universally conserved Zn²⁺ in AlaRS-Ed protects its proofreading activity from reactive oxygen species (ROS) to maintain high fidelity Ala-codons translation, necessa

SUBMITTER: Gogoi J 

PROVIDER: S-EPMC12003907 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature