tRNA (adenine(37)-N6)-methyltransferase (TRMO)

tRNA (adenine(37)-N6)-methyltransferase (TRMO) is an enzyme responsible for the methylation of adenine at the N6 position at the 37th nucleotide of certain tRNAs, a modification critical for the maintenance of correct codon–anticodon pairing and translational fidelity during protein synthesis. Like other tRNA methyltransferases, TRMO is a member of the class I methyltransferase family, characterized by the Rossmann-like fold. Its activity ensures proper tRNA structure and function, preventing translational errors. Aberrant function or misregulation of tRNA-modifying enzymes, including TRMO, has been linked to human diseases such as cancer and metabolic impairment through the disruption of normal translational fidelity and protein homeostasis[1][2][4]. TRMO shares sequence and structural features with other methyltransferases and is essential for normal cellular biosynthetic processes.

Other names

tRNA methyltransferase OC9orf156HSPC219NAP1Nef (lentivirus myristoylated factor) associated protein 1nef-associated protein 1thioesterase NAP1

Catalyzes N6-methylation of adenine(37) in tRNA, facilitating proper decoding and translation; may regulate the stability and function of tRNA