PRMT5 in mitochondria regulates mtDNA stability through TFAM arginine methylation - PubMed
5 hours ago
- #DNA stability
- #protein methylation
- #mitochondria
- PRMT5, a protein arginine methyltransferase, localizes to mitochondria and is crucial for mtDNA stability.
- PRMT5 knockout cells show reduced mtDNA copy numbers, impaired mitochondrial function, and increased sensitivity to mtDNA-damaging agents.
- TFAM is identified as a new interacting partner of PRMT5, with methylation at R82 residue being essential for mtDNA binding and protection.
- Defective R82-methylation leads to TFAM destabilization and degradation by LonP1, impacting mtDNA maintenance.
- The study highlights PRMT5's role in mitochondrial DNA homeostasis and its implications for cell survival and mitochondrial plasticity.