{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSUPV3L1 encodes an evolutionarily conserved ATP‐dependent DExH‐box helicase predominantly localized in the mitochondrial matrix. Studies have demonstrated that this enzyme, also known as hSuv3p, unwinds double‐stranded RNA and DNA substrates in a 5′–3′ direction using energy from ATP hydrolysis, with its activity being modulated by nucleic acid binding and divalent cations. Such biochemical properties underpin its essential role in the surveillance and turnover of mitochondrial RNAs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSUPV3L1 assembles with polynucleotide phosphorylase (PNPase) to form the mitochondrial degradosome, a specialized complex responsible for the efficient degradation of structured RNA species. The enzymatic activity of SUPV3L1 is greatly enhanced in its dimeric state—in part mediated by a distinct C‐terminal tail—which is critical for persistent RNA binding and for productive interactions with PNPase. This degradosome not only facilitates the removal of aberrant and decay‐intermediate RNAs but also collaborates with the mitochondrial polyadenylation polymerase (mtPAP) to finely regulate the poly(A) tail lengths of mitochondrial mRNAs, thereby ensuring mitochondrial protein synthesis and overall organelle homeostasis. Loss or dysfunction of SUPV3L1 results in the accumulation of RNA decay intermediates, impaired mitochondrial function, and even compromised energy production."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "11"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEmerging evidence further implicates SUPV3L1 in additional aspects of cellular regulation beyond mitochondrial RNA decay. A subset of studies has revealed a nuclear presence—particularly within the nucleolus—where SUPV3L1 may participate in regulating cell cycle progression and maintaining genomic stability through interactions with other genome-protecting helicases. Structural investigations have underscored the importance of its dimerization for robust RNA binding and degradosome assembly. Clinically, mutations leading to disruption or C-terminal truncation of SUPV3L1 are associated with neurodegenerative phenotypes featuring mitochondrial dysfunction, thereby highlighting its critical role in both cellular homeostasis and human disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "15"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Michal Minczuk, Jan Piwowarski, Monika A Papworth, et al. 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