Methionyl-tRNA synthetase 1 (MARS1)

Methionyl-tRNA synthetase 1 (MARS1) is a cytosolic enzyme that catalyzes the ligation of methionine to its cognate tRNA, an essential first step for translation initiation and protein biosynthesis[6][4]. It is a member of the class I aminoacyl-tRNA synthetase family, part of the multi-tRNA synthetase complex (MSC), and contains domains for protein-protein interactions and for catalysis of aminoacyl-tRNA formation[1][4]. Beyond its core enzymatic function, MARS1 is implicated in cell cycle regulation, oxidative stress response, and cancer biology through phosphorylation-mediated regulatory mechanisms and stabilization of cyclin-dependent kinase 4 (CDK4)[5]. Pathogenic mutations in MARS1 are causally linked to axonal neuropathy such as Charcot-Marie-Tooth disease type 2U and interstitial lung and liver disease, underscoring its significance in human health and disease[6].

Other names

Methionine--tRNA ligase, cytoplasmicMARSMetRSSPG70CMT2Umethionine tRNA ligase 1, cytoplasmicILFS2ILLDMETRSMRSMTRNSTTD9

Inhibition of enzyme activity (blocking methionine ligation to tRNA); Allosteric modulation of substrate binding; Disrupting MARS1–protein interactions affecting cell cycle and redox states[5]