Tyrosine--tRNA ligase, cytoplasmic (YARS1 (also commonly referred to as TyrRS))

Tyrosine--tRNA ligase, cytoplasmic (YARS1), also known as tyrosyl-tRNA synthetase or TyrRS, is an essential enzyme that catalyzes the two-step attachment of L‑tyrosine to its cognate tRNATyr during protein biosynthesis. This reaction is fundamental for translating genetic information into proteins by ensuring accurate incorporation of tyrosine at positions specified by mRNAs. The enzyme first activates tyrosine with ATP forming a Tyr‑AMP intermediate before transferring it onto tRNATyr. Beyond this canonical role in translation, YARS1 has additional functions including regulation of nuclear poly(ADP-ribosyl)ation through interaction with PARP1—especially upon binding small molecules such as resveratrol—and may exert cytokine-like or proangiogenic effects via proteolytic fragments outside the context of protein synthesis[1][3][4][6].

Other names

Tyrosyl-tRNA synthetaseYARS1SYYC_HUMAN (UniProt entry name)EC 6.1.1.1

For inhibitors like resveratrol: - Inhibition of aminoacylation activity by direct binding, leading to relocalization from cytoplasm to nucleus where it stimulates PARP1-mediated poly(ADP-ribosyl)ation independent of aminoacylation function[1].