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Novel Aspects of Polynucleotide Phosphorylase Function in Streptomyces [PDF]

open access: goldAntibiotics, 2018
Polynucleotide phosphorylase (PNPase) is a 3′–5′-exoribnuclease that is found in most bacteria and in some eukaryotic organelles. The enzyme plays a key role in RNA decay in these systems.
George H. Jones
doaj   +4 more sources

Polynucleotide phosphorylase has an impact on cell biology of Campylobacter jejuni [PDF]

open access: goldFrontiers in Cellular and Infection Microbiology, 2012
Polynucleotide phosphorylase, encoded by the pnp gene, is known to degrade mRNA, mediating post-transcriptional regulation and may affect cellular functions. The role of PNPase is pleiotropic.
Nabila eHaddad   +12 more
doaj   +6 more sources

Identification of genes potentially regulated by human polynucleotide phosphorylase (hPNPase old-35) using melanoma as a model. [PDF]

open access: yesPLoS ONE, 2013
Human Polynucleotide Phosphorylase (hPNPase(old-35) or PNPT1) is an evolutionarily conserved 3'→ 5' exoribonuclease implicated in the regulation of numerous physiological processes including maintenance of mitochondrial homeostasis, mtRNA import and ...
Upneet K Sokhi   +8 more
doaj   +6 more sources

Polynucleotide phosphorylase protects against renal tubular injury via blocking mt-dsRNA-PKR-eIF2α axis [PDF]

open access: yesNature Communications, 2023
Renal tubular atrophy is a hallmark of chronic kidney disease. The study by Zhu et al. reveals the protective role of tubular polynucleotide phosphorylase (PNPT1) against renal atrophy by blocking the leakage of mitochondrial dsRNAs into cytoplasm where ...
Yujie Zhu   +12 more
doaj   +3 more sources

Polynucleotide Phosphorylase Mediates a New Mechanism of Persister Formation in Escherichia coli [PDF]

open access: yesMicrobiology Spectrum, 2023
Despite the identification of many genes and pathways involved in the persistence phenomenon in bacteria, the mechanisms of persistence are not well understood.
Nan Wu   +8 more
doaj   +3 more sources

Pseudomonas aeruginosa Polynucleotide Phosphorylase Contributes to Ciprofloxacin Resistance by Regulating PrtR [PDF]

open access: yesFrontiers in Microbiology, 2019
Pseudomonas aeruginosa is an opportunistic bacterial pathogen that causes various acute and chronic infections. It is intrinsically resistant to a variety of antibiotics. However, production of pyocins during SOS response sensitizes P.
Zheng Fan   +11 more
doaj   +3 more sources

Functions of Conserved Domains of Human Polynucleotide Phosphorylase on RNA Oxidation. [PDF]

open access: hybridInsights Biomed Res, 2019
Human polynucleotide phosphorylase (hPNPase), an exoribonuclease that is primarily localized in mitochondria, plays an important role in reducing oxidized RNA and protecting cells under oxidative stress conditions. hPNPase contains two catalytic domains (
Malla S, Li Z.
europepmc   +4 more sources

Rapid and scalable detection of synthetic mRNA byproducts using polynucleotide phosphorylase and polythymidine oligonucleotides [PDF]

open access: yesRNA Biology
Production and storage of synthetic mRNA can introduce a variety of byproducts which reduce the overall integrity and functionality of mRNA vaccines and therapeutics.
Francis Combes   +3 more
doaj   +3 more sources

Polynucleotide phosphorylase: Not merely an RNase but a pivotal post-transcriptional regulator. [PDF]

open access: yesPLoS Genetics, 2018
Almost 60 years ago, Severo Ochoa was awarded the Nobel Prize in Physiology or Medicine for his discovery of the enzymatic synthesis of RNA by polynucleotide phosphorylase (PNPase).
Todd A Cameron   +2 more
doaj   +3 more sources

Selective 8-oxo-rG stalling occurs in the catalytic core of polynucleotide phosphorylase (PNPase) during degradation. [PDF]

open access: hybridProc Natl Acad Sci U S A
Significance Polynucleotide phosphorylase (PNPase) is a widely conserved exoribonuclease that degrades single-stranded RNA transcripts in the 3′ to 5′ direction, forming single-nucleotide diphosphates and a short oligonucleotide product.
Miller LG   +14 more
europepmc   +4 more sources

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