{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRMT10C, also known as mitochondrial RNase P protein 1 (MRPP1), plays a central role in the early steps of mitochondrial RNA maturation. As part of the heterotrimeric mtRNase P complex—which also contains MRPP2 and MRPP3—it catalyzes the 5′-end cleavage of precursor tRNAs from long polycistronic transcripts and contributes to processing mitochondrial long noncoding RNAs. These processing events are crucial for proper mitochondrial gene expression, RNA modification, translation, and respiratory function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural studies have revealed that TRMT10C, in complex with SDR5C1 (MRPP2), forms a subcomplex that recognizes and binds conserved mitochondrial tRNA elements—including the anticodon loop—to appropriately position substrates for methylation. The MRPP1–MRPP2 duo not only catalyzes the N1-methylation (m¹A/m¹G) at position 9 of tRNAs using S-adenosyl-l-methionine as a methyl donor, but also functions as a processing platform that can retain the tRNA product after 5′-cleavage, thereby enhancing subsequent 3′-end maturation events. These coordinated activities ensure the correct folding and function of mitochondrial tRNAs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDefects in TRMT10C function, such as those caused by pathogenic mutations, result in decreased protein stability and impaired processing of mitochondrial RNA substrates, leading to the accumulation of unprocessed precursors, defective tRNA methylation, and compromised mitochondrial protein synthesis. Such mutations have been linked to early-onset mitochondrial disease phenotypes and, in other contexts, dysregulation of TRMT10C has been associated with altered cell proliferation and migration in gynecological cancers. Moreover, while interactions with deleterious peptides like amyloid‑β may inhibit associated RNA processing activities, these effects do not appear to be specific to TRMT10C, underscoring its critical role in mitochondrial function and cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Maria I G Lopez Sanchez, Tim R Mercer, Stefan M K Davies, et al. 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