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Literature summary for 2.7.7.8 extracted from

  • Malla, S.; Li, Z.
    Functions of conserved domains of human polynucleotide phosphorylase on RNA oxidation (2019), Insights Biomed. Res., 3, 62-67 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in HeLa cell Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information expression of polynucleotide phosphorylase mutants lacking specific functional domains, i.e., mitochondrial translocation signal (MTS), catalytic domains (RPH1 and RPH2) and RNA binding domains (KH and S1), in cultured HeLa cells. MTS is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine in mitochondria, but not in cytoplasm. Both RPH1 or RPH2 domain alone are able to support the full activity of polynucleotide phosphorylase in reducing 8-hydrooxyguanosine during oxidative stress, and the S1 RNA-binding domain, but not KH, is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine under oxidative stress Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q8TCS8
-
-

General Information

General Information Comment Organism
physiological function polynucleotide phosphorylase is involved in controlling the levels of RNA oxidation marker 8-hydrooxyguanosine in both cytoplasmic and mitochondrial fractions. Expression of exogenous polynucleotide phosphorylase reduces 8-hydrooxyguanosine levels in both cytoplasm and mitochondria. The S1 RNA binding domain is crucial for reducing 8-hydrooxyguanosine in both cytoplasm and mitochondria, while the N-terminal mitochondrial translocation signal is required for 8-hydrooxyguanosine reduction in mitochondria. One of the RPH1 or RPH2 domains is sufficient to reduce 8-hydrooxyguanosine levels in RNA under oxidative stress conditions Homo sapiens