tRNA (guanine(26)-N(2))-dimethyltransferase (TRMT1)

tRNA (guanine(26)-N(2))-dimethyltransferase (TRMT1) is an enzyme responsible for catalyzing the formation of N2,N2-dimethylguanosine (m(^{2,2})G) at position 26 in both cytoplasmic and mitochondrial tRNAs[4][5]. This modification supports efficient protein translation and helps maintain redox homeostasis in cells, protecting them against oxidative stress[1][4]. TRMT1 contains a C-terminal zinc finger motif critical for its function, uses S-adenosyl methionine as a methyl donor, and its deficiency or mutation results in decreased tRNA methylation, lowered protein synthesis, higher oxidative stress, and is implicated in certain forms of autosomal recessive intellectual disorder[4][5]. The enzyme is a direct human substrate for SARS-CoV-2 main protease (Mpro), which can cleave and inactivate TRMT1, further highlighting its importance in cell biology and stress responses[1][3].

Other names

tRNA methyltransferase 1hTRM1FLJ20244TRM1tRNA 2,2-dimethylguanosine-26 methyltransferasetRNA(guanine-26,N(2)-N(2)) methyltransferasetRNA(m(2,2)G26)dimethyltransferaseMRT68N(2),N(2)-dimethylguanosine tRNA methyltransferaseTRMT1 homolog