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- Table of Contents
Facts about Polyribonucleotide nucleotidyltransferase 1, mitochondrial.
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. Required for proper processing and polyadenylation of mitochondrial mRNAs.
Mouse | |
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Gene Name: | Pnpt1 |
Uniprot: | Q8K1R3 |
Entrez: | 71701 |
Belongs to: |
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polyribonucleotide nucleotidyltransferase family |
DKFZp762K1914; EC 2.7.7; EC 2.7.7.8; mitochondrial; OLD35; old-35; PNPase 1; PNPase old-35; PNPase; Polynucleotide phosphorylase 1; Polynucleotide phosphorylase-like protein; polyribonucleotide nucleotidyltransferase 1
Mass (kDA):
85.683 kDA
Mouse | |
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Location: | 11|11 A3.3 |
Sequence: | 11; |
PNPT1 is an enzyme from the mitochondrial genome that is involved in a phosphate-dependent three-prime-to-five-prime RNA exonuclease reaction. It is also a subunit of the exosome complex and is a marker for mitochondria. ELISA kits are available to detect this enzyme and corresponding metabolites.
PNPT1 is a phosphatase-dependent 3'-to-5-prime RNA exopeptidase found in Escherichia coli. It has been found to be involved in double-strand break repair, facilitate the localization of RecN, and co-purify with RecA. It extends 3'-OH ends of RNA, and may function as a protein chaperone.
This gene codes for a phosphate-dependent 3-primase that encoding this enzyme is essential for cell survival. In addition, PNPT1 has been found to be involved in the regulation of RNA damage by other proteins. This enzyme is also involved in gene repair and DNA repair. When activated, PNPT1 kills DNA damage by degrading DNA.
PNPT1 is an essential component of the ribosomal subunit 40S. It interacts with histones H2A and H2B, regulating nucleosome disassembly and transcription elongation. This enzyme also acts as a component of the Polycomb group PRC1 complex, which promotes transcription of DNA packaged into chromatin.
In addition to its role in RNA translation, PNPT1 is also a phosphate-dependent 3-prim-to-5-prime RNA exopeptidase. It is an important RNA exonuclease in human cells. In fact, a phosphate-dependent enzyme is essential in the repair of DNA damage caused by RNA.
In the exosome complex, the enzyme PNPT1 is involved in 3-prime-to-5-prime exoribonuclease activity. It also has roles in RNA processing and degradation. hPNPase is a mitochondrial RNA-processing enzyme that is localized in the intermembrane space and has an essential role in maintaining the mitochondria's homeostasis. Moreover, hPNPase is implicated in tumorigenesis and cellular responses to a viral infection.
A synthetic peptide that recognizes PNPT1 has been developed for use with the anti-PNPT1 antibody, manufactured by Aviva Systems Biology. It may interfere with anti-PNPT1 antibody binding in immunohistochemistry and western blot. Therefore, this peptide should be used with caution. This product is not approved for therapeutic use. It is intended for research purposes.
RNA processing plays a major role in the expression of genetic information. In eukaryotes, mRNA decay involves two major pathways. One is initiated by poly(A) shortening, and the other pathway involves 3' to 5' exonucleolytic degradation. Both pathways involve the exosome. The exosome also participates in processing small nucleolar RNAs and nuclear RNAs. Furthermore, the exosome also processes non-coding RNAs, such as those arising from bidirectional transcription from enhancers.
PNPT1 is a mitochondrial protein that has recently attracted attention for its role in mitophagy. It is a highly conserved protein found in most cell types and has a role in the regulation of cellular metabolism. It has been shown to be a marker of mitochondrial biogenesis. However, it is not known exactly where it resides in the cell. To answer this question, we have analyzed the structure of PNPT1 and its functional role in the mitochondria.
PNPT1 is a component of the exosome complex and is involved in RNA processing and degradation. It is located within the mitochondrial intermembrane space and is known to be implicated in hereditary hearing loss. Mutations in this gene may lead to a range of diseases, including mitochondrial disease. The mutation may lead to a loss of function in a person who is already suffering from this disease.
The mutation of PNPT1 caused the accumulation of dsRNA in the cells of fast-proliferating HeLa and EndoC-bh2 strains. Interestingly, dsRNA was not generated in the cells of the same cell line when PNPT1 was silenced for 48 h. This finding is not explained by the editing of ADAR, and double knockdown of PNPT1 and SUV3 failed to induce dsRNA accumulation in EndoC-bh2 cells either.
Human PNPT1 ELISA Kits are used to measure the level of PNPT1 in plasma, serum, cell culture supernates, and tissue samples. The kit contains a standard, which can be a natural or recombinant protein, expressed in a mammalian cell, yeast, or E. coli. The kit also contains sodium azide and a diluent solution.
GeneTex SARS-CoV-2 (COVID-19) Nucleocapsid Protein Sandwich ELISA Kit is a ready-to-use in vitro assay. It enables highly sensitive detection of SARS-CoV-2 virus N protein. Its detection limit is less than 18 pg/ml, and it can be completed in less than four hours.
The PNPT1 gene encodes a polynucleotide phosphorylase protein (PNPASE), which regulates the import of RNA into mitochondria. It is involved in the inflammatory process induced by IFNs. In addition to its role in mitochondrial function, PNPT1 has been associated with hereditary hearing loss. Therefore, PNPT1 is a useful marker for evaluating hearing loss in patients with this disorder.
The PNPT1 gene, located at the centromeric end of chromosome 2, is one of the most commonly studied proteins in human cancers. Its function is unclear but it is implicated in cell cycle regulation and malignancy. Sokhi et al. suggested that the gene plays a role in regulating cell division and cell cycle. In this study, we confirmed the localization of the PNPT1 gene, which co-immunoprecipitates with AGO1x in nuclear extracts.
The PNPT1 protein has a monomer structure with two RNase-PH domains and an RNA binding domain. The human and zebrafish PNPase share a high degree of conservation, with 70 percent identity. It is also predicted to contain a mitochondrial targeting sequence. The recombinant PNPase contains a V5-His tag and has a higher molecular mass. Using a PeptideMass online calculation tool, we calculated the protein mass of the recombinant PNPase. Besides PNPase, we also detected the heat-shock protein 60, another marker of mitochondria.
A human pNPase RNA was immunoblotted with mitochondria expressing WT and the p.Glu475Gly mutation. This reaction was repeated with 1x and 2x amounts of RNA. The RNA-bound RNase P was two times lower in PNPT1-mutant mitochondria. This result indicates that the gene is partially functional for RNA import in yeast cells.
The Boster Bio PNPT1 marker is a highly sensitive and specific gene expression assay for melanoma. This assay is capable of detecting cancer cells in a wide range of tissues, including melanocytes, keratinocytes, and squamous cell carcinoma. The gene is expressed in both normal and malignant melanoma cells.
PMID: 12419256 by Raijmakers R., et al. Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring.
PMID: 16966381 by Chen H.W., et al. Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis.