Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Definition:

RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.

References:

[1]. Geng Wang, et al. PNPASE regulates RNA import into mitochondria. Cell. 2010 Aug 6;142(3):456-67. [Content Brief]

[2]. Jan Piwowarski, et al. Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria. J Mol Biol. 2003 Jun 20;329(5):853-7. [Content Brief]

[3]. Shimyn Slomovic, et al. Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA. RNA. 2008 Feb;14(2):310-23. [Content Brief]

[4]. Zbigniew Pietras, et al. Dedicated surveillance mechanism controls G-quadruplex forming non-coding RNAs in human mitochondria. Nat Commun. 2018 Jul 2;9(1):2558. [Content Brief]

[5]. Devanand Sarkar, et al. Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence. Mol Cell Biol. 2005 Aug;25(16):7333-43. [Content Brief]

[6]. Jinhua Wu, et al. Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress. Biochem Biophys Res Commun. 2008 Jul 25;372(2):288-92. [Content Brief]

[7]. Samuel W French, et al. The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity. Cancer Lett. 2007 Apr 18;248(2):198-210. [Content Brief]

[8]. Swadesh K Das, et al. Human polynucleotide phosphorylase selectively and preferentially degrades microRNA-221 in human melanoma cells. Proc Natl Acad Sci U S A. 2010 Jun 29;107(26):11948-53. [Content Brief]

[9]. Devanand Sarkar, et al. Down-regulation of Myc as a potential target for growth arrest induced by human polynucleotide phosphorylase (hPNPaseold-35) in human melanoma cells. J Biol Chem. 2003 Jul 4;278(27):24542-51. [Content Brief]

[10]. D Sarkar, et al. Defining the mechanism by which IFN-beta dowregulates c-myc expression in human melanoma cells: pivotal role for human polynucleotide phosphorylase (hPNPaseold-35). Cell Death Differ. 2006 Sep;13(9):1541-53. [Content Brief]

[11]. Victoria Portnoy, et al. Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts. RNA. 2008 Feb;14(2):297-309. [Content Brief]

[12]. Dennis Ding-Hwa Wang, et al. Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality. J Biol Chem. 2009 Jul 31;284(31):20812-21. [Content Brief]

[13]. Magdalena Leszczyniecka, et al. Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16636-41. [Content Brief]

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