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Ribonuclease P protein subunit p20 (POP7) is a highly conserved protein encoded by the POP7 gene. It acts as an essential component of the eukaryotic ribonuclease P and ribonuclease MRP complexes, responsible for the endonucleolytic cleavage of precursor tRNA and pre-rRNA, respectively. These enzymatic processes are indispensable for the maturation of tRNAs and functional ribosome biogenesis. Located predominantly in the nucleolus, POP7 binds nucleic acids and stabilizes the structure of these ribonucleoprotein complexes, directly contributing to their catalytic activity. Genetic mutations or dysregulation of POP7 are implicated in rare skeletal dysplasias and may influence cancer progression through post-transcriptional mRNA regulation[1][3][4][5][6][7][8].
No established drugs; hypothetical mechanisms include inhibition/modulation of RNA processing through binding to POP7 or its complex
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