Tyrosyl-tRNA synthetase (TyrRS (or YARS))

Tyrosyl-tRNA synthetase is an enzyme essential for protein synthesis, catalyzing the ATP-dependent attachment of tyrosine to its corresponding tRNA (tRNA^Tyr)[2][6]. This reaction is crucial for translating the genetic code into functional proteins. Structurally, TyrRS is a class I aminoacyl-tRNA synthetase, typically found as a homodimeric protein with a characteristic catalytic domain (Rossmann fold) and tRNA anticodon recognition elements[2][1]. In mitochondria, some isoforms contribute to both tRNA charging and RNA splicing. Noncanonical functions in humans include roles in organizing the actin cytoskeleton, with mutations in YARS1 implicated in inherited neurodegenerative diseases such as Charcot–Marie–Tooth neuropathy[4]. While not a major direct pharmacological target in humans, TyrRS is a validated target for antimicrobial drug development due to the reliance of many pathogens on their own TyrRS activity for survival[3].

Other names

Tyrosine--tRNA ligaseYARSTyrosine--tRNA synthetaseTyrosyl-tRNA ligaseTyrosyl-tRNA synthetase 1 (YARS1)

Inhibition of TyrRS interferes with the aminoacylation of tRNA^Tyr, halting protein synthesis and leading to cell death (antibacterial/antifungal action) - Potential modulation of actin organization in cellular/neurological contexts