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RNA oxidation: Role of polynucleotide phosphorylase in the quality control of oxidized RNA

JoLS, Journal of Life Sciences, 2021
Reactive oxygen species is one of the most common cellular RNA damaging agents in living organisms. A growing number of studies show a strong correlation between oxidatively damaged RNA and human diseases, predominantly age-related neurodegenerative ...
Sulochan Malla, Alexander Kwakye
semanticscholar   +1 more source

Mechanism of polynucleotide phosphorylase

Biochemistry, 1989
The de novo polymerization of RNA initiated by polynucleotide phosphorylase from nucleoside diphosphates was examined. End group analysis performed under conditions designed to specifically end label the polymer revealed no evidence for a 5'-pyrophosphate-terminated polymer.
M, Sulewski   +3 more
openaire   +2 more sources

Human polynucleotide phosphorylase: location matters

Trends in Cell Biology, 2007
Human polynucleotide phosphorylase (hPNPase) is an RNA-processing enzyme induced in response to type I interferons and during terminal differentiation and cellular senescence. hPNPase was thought to contribute to cellular senescence through its RNA-degrading activity in the cytosol; however, recent studies show that hPNPase localizes to the ...
Hsiao-Wen, Chen   +2 more
openaire   +2 more sources

Photometric Assay for Polynucleotide Phosphorylase

Analytical Biochemistry, 1999
Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs. It is also believed to play a key role in turnover of prokaryotic transcripts, thus regulating gene expression. At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve ...
L, Fontanella   +5 more
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Polynucleotide phosphorylase from plant cells

Plant Cell Reports, 1984
The isolation of polynucleotide phosphorylase (EC 2. 7. 7. 8) from suspension cultured plant cells of parsley (Petroselinum sativum) and from tomato seedlings (Lycopersicon esculentum) is described. The procedure includes an ultracentrifugation step, a glycerol density gradient centrifugation and preparative gel electrophoresis under nondenaturing ...
E, Schumacher-Wittkopf   +2 more
openaire   +2 more sources

Polynucleotide Phosphorylase and the T3SS

2007
Low temperatures as well as encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. The exoribonuclease polynucleotide phosphorylase (PNPase) has previously been shown to be required by several species of bacteria, including Yersinia, for low-temperature growth. We have shown that PNPase also
Jason A, Rosenzweig, Kurt, Schesser
openaire   +2 more sources

The origin of polynucleotide phosphorylase domains

Molecular Phylogenetics and Evolution, 2004
In this report, we document the presence of polynucleotide phosphorylase (PNPase) in the animal eukaryotes. These proteins contain several domains, including 2 RNase PH domains (PNPase 1 and PNPase 2) which are closely related functionally and in sequence similarity to ribonuclease PH (RPH) protein.
Magdalena, Leszczyniecka   +3 more
openaire   +2 more sources

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