2019
DOI: 10.36959/584/448
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Functions of Conserved Domains of Human Polynucleotide Phosphorylase on RNA Oxidation

Abstract: PNPase is an evolutionarily conserved 3' → 5' exoribonuclease that participates in RNA metabolism and regulates diverse physiological processes including cellular senescence and homeostasis [10][11][12][13][14][15]. The human PNPase (hPNPase) contains two RPH catalytic domains and an α-helix in between them occupying the N-terminal two-third of the protein, and KH and S1 RNA binding domains (KH and S1) at the C-terminal. In addition, a mitochondrial-targeting

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Cited by 3 publications
(2 citation statements)
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“…Locating the oxidation sites with or without protein presence could also help answer this query. Increased fragmentation of oxidized RNA in the cellular conditions might be due to the higher affinity of oxidized RNA to enzymes such as polynucleotide phosphorylase leading to RNA degradation ( Hayakawa et al, 2001 ; Malla and Li, 2019 ).…”
Section: Discussionmentioning
confidence: 99%
“…Locating the oxidation sites with or without protein presence could also help answer this query. Increased fragmentation of oxidized RNA in the cellular conditions might be due to the higher affinity of oxidized RNA to enzymes such as polynucleotide phosphorylase leading to RNA degradation ( Hayakawa et al, 2001 ; Malla and Li, 2019 ).…”
Section: Discussionmentioning
confidence: 99%
“…Loss of these modifications would be expected to adversely affect those functions during cellular translation, thereby making such tRNA targets for degradation. Indeed, the growth delay effect observed soon after UVR exposure could be related to the clearing of damaged tRNA [65] following recognition and binding by proteins such as polynucleotide phosphorylase in E. coli [77,78] and potentially YB-1 protein in humans [79] for subsequent turnover by RNA degradation machinery in E. coli [80,81] and the eukaryotic exosome [82]. However, further studies are required to understand the fate of cellular tRNA that has undergone partial degradation of PTMs and their relationship to the oxidation of canonical bases such as guanosine.…”
Section: Potential Consequences On Trna Due To Photooxidative Degradation Of Ptmsmentioning
confidence: 99%