tRNA methyltransferase 10C, mitochondrial RNase P subunit (TRMT10C)

TRMT10C (tRNA methyltransferase 10C, mitochondrial RNase P subunit) is a mitochondrial enzyme that forms a subcomplex with SDR5C1 (dehydrogenase) and, as part of mitochondrial RNase P, plays a critical role in mitochondrial tRNA maturation[1][7]. It catalyzes the SAM-dependent methylation of the nitrogen-1 (N1) position on purine (adenine or guanine) at position 9 in mitochondrial tRNA, a modification essential for correct tRNA folding and stability[1][6][7]. TRMT10C, also referred to as MRPP1, acts together with its partners in the cleavage of 5’ leaders from mitochondrial tRNAs and coordinates subsequent processing steps including 3’ cleavage and CCA addition, which are prerequisites for effective mitochondrial translation and thus energy metabolism[1][7]. Pathogenic variants in TRMT10C cause fatal or severe mitochondrial disorders, notably combined oxidative phosphorylation deficiency type 30 (COXPD30)[5]. No drugs are presently approved for specific modulation of TRMT10C function, and its loss leads to defects in mitochondrial gene expression and multi-organ dysfunction[1][5][7].

Other names

MRPP1RG9MTD1Mitochondrial RNase P protein 1mitochondrial ribonuclease P protein 1tRNA methyltransferase 10 homolog CCOXPD30RNA (guanine-9-)-methyltransferase domain-containing 1mRNA methyladenosine-N(1)-methyltransferaseHBV pre-S2 trans-regulated protein 2Renal carcinoma antigen NY-REN-49FLJ20432tRNA (adenine(9)-N(1))-methyltransferasetRNA (guanine(9)-N(1))-methyltransferaseD16Ertd454eHNYARnmtd1

Not applicable (no specific drugs known to directly target TRMT10C)