tRNA methyltransferase 1-like protein (TRMT1L)

tRNA methyltransferase 1-like protein (TRMT1L) is an RNA-modifying enzyme that specifically dimethylates a guanine residue at position 27 of tyrosine tRNA (tRNA^Tyr) using S-adenosyl-L-methionine as the methyl group donor[1][2][4]. This modification, N2,N2-dimethylguanosine (m^2,2G), is critical for the stability and translational function of tRNA, particularly for tyrosine and serine codons[1]. TRMT1L is also required for maintaining another modification, acp3U, in the D-loop of several cytoplasmic tRNAs. Loss of TRMT1L activity results in reduced levels of certain tRNAs and is linked to impaired neuronal function and developmental disorders in humans; mouse models show that the gene is involved in motor coordination and postnatal brain function[1][2]. The enzyme operates in parallel with its paralog, TRMT1, which modifies a nearby guanine at position 26 of tRNA^Tyr[1]. No direct drug interactions or biomarker roles are currently described for TRMT1L.

Other names

tRNA (guanine(27)-N(2))-dimethyltransferaseTRMT1LC1orf25TRM1LMSTP070TRMT1-like proteintRNA methyltransferase 1-like proteinTRM1-likebG120K12.3TRM1 tRNA methyltransferase 1-liketRNA methyltransferase 1 homolog-liketRNA methyltransferase 1 like