tRNA methyltransferase activator subunit 11-2 (TRMT112)

**tRNA methyltransferase activator subunit 11-2 (TRMT112)** is a small, highly conserved protein that functions primarily as an allosteric activator and stabilizing cofactor for several S-adenosyl-L-methionine (SAM)-dependent methyltransferases in eukaryotic and archaeal cells[1][2][3]. These methyltransferases collectively modify a variety of substrates, including tRNAs, rRNAs, and protein factors, thereby playing central roles in RNA maturation, translation, and overall cellular metabolism. TRMT112 is structurally characterized by a zinc-binding domain (ZBD) and a central domain (although the human ZBD does not coordinate a zinc ion). In human cells, TRMT112 has been identified as a necessary partner for a range of methyltransferases, including TRMT11, WBSCR22, MTQ2/HemK2, METTL5, ALKBH8, and TRMT9B, each participating in methylation reactions at specific nucleotide or protein residues that are crucial for efficient and accurate gene expression[1][2]. By itself, TRMT112 is not directly involved in catalyzing methylation but is required for the stability, catalytic activity, and substrate interaction of its methyltransferase partners. Disruptions in the function or expression of TRMT112 or its associated complexes have been implicated in various diseases, including certain cancers and neurological syndromes, due to their downstream effects on RNA processing, translation, and cell growth[1].

Other names

Multifunctional methyltransferase subunit TRM112-like proteinTRM112TRMT11-2hTrm112tRNA methyltransferase 112 homologAD-001HSPC152HSPC170TRMT11-2 homologTRM112-like protein

Not applicable; TRMT112 is not a direct drug target but rather a cofactor/activator for multiple methyltransferases