Mitochondrial polyribonucleotide nucleotidyltransferase, also designated 3'-5' RNA exonuclease, OLD35, PNPase or PNPT1, is an evolutionaly conserved protein in which the mouse protein shares 90% identity with the human version. PNPase participates in mRNA degradation and hydrolyzes single-stranded ribonucleotides in the 3' to 5' direction. PNPase forms homotrimers and is upregulated in response to interferon-β induction. The N-terminus of PNPase contains a putative mitochondrial targeting sequence; mutation analysis confirms that N-terminal sequences of PNPase target the protein to the mitochondria. Endogenous PNPase also co-localizes with a mitochondrial marker protein in HeLa cells.
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Mitochondrial polyribonucleotide nucleotidyltransferase, also designated 3'-5' RNA exonuclease, OLD35, PNPase or PNPT1, is an evolutionaly conserved protein in which the mouse protein shares 90% identity with the human version. PNPase participates in mRNA degradation and hydrolyzes single-stranded ribonucleotides in the 3' to 5' direction. PNPase forms homotrimers and is upregulated in response to interferon-β induction. The N-terminus of PNPase contains a putative mitochondrial targeting sequence; mutation analysis confirms that N-terminal sequences of PNPase target the protein to the mitochondria. Endogenous PNPase also co-localizes with a mitochondrial marker protein in HeLa cells.
