Recombinant Human PNPT1 protein is a Human Full Length protein, in the 46 to 783 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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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 (PubMed:29967381). 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.
PNPASE, PNPT1, 3'-5' RNA exonuclease OLD35, PNPase old-35, Polynucleotide phosphorylase 1, Polynucleotide phosphorylase-like protein, PNPase 1
Recombinant Human PNPT1 protein is a Human Full Length protein, in the 46 to 783 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 7.4
Constituents: 89% PBS, 10% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab202628 was purified by conventional chromatography techniques.
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 (PubMed:29967381). 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.
Belongs to the polyribonucleotide nucleotidyltransferase family.
PNPT1 also known as polyribonucleotide nucleotidyltransferase 1 or mitochondrial RNA polymerase is an enzyme with a molecular weight of approximately 85 kDa. The protein is widely expressed in cellular mitochondria and cytoplasm where it performs its essential functions in RNA processing. It aids in the degradation and processing of mitochondrial RNA reflecting its significant role in mitochondrial function. The protein's activity relies heavily on its conserved domains that are necessary for effective RNA binding and hydrolysis.
PNPT1 plays a critical role in maintaining mitochondrial gene expression and is a component of the RNA-degrading exosome complex. This complex is involved in the surveillance and breakdown of defective RNA molecules thereby ensuring the integrity and balance of the mitochondrial transcriptome. By participating in these processes PNPT1 helps to enhance the overall mitochondrial function which is vital for energy production and cell metabolism.
PNPT1 significantly contributes to the mitochondrial RNA decay pathway and the broader RNA processing pathways related to mitochondrial maintenance. It interacts with other proteins such as polynucleotide phosphorylase domain-containing proteins which are involved in similar RNA processing functions. This integration highlights the coordinated network of proteins that cooperate to ensure proper mitochondrial RNA metabolism affecting both the quality and quantity of the RNA molecules available for translation.
Mutations or dysregulations in PNPT1 are linked to mitochondrial disorders such as autosomal recessive combined oxidative phosphorylation deficiency. These disorders often exhibit symptoms like muscle weakness developmental delays and other systemic issues due to compromised energy production. Additionally studies indicate a possible connection between PNPT1 dysfunction and neurodegenerative disorders where its interaction with proteins like TYMP (thymidine phosphorylase) can lead to mitochondrial dysfunction and subsequent disease progression.
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15% SDS-PAGE analysis of ab202628 (3μg).
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