Functions of Conserved Domains of Human Polynucleotide Phosphorylase on RNA Oxidation. [PDF]
Insights 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.
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Polynucleotide phosphorylase promotes the stability and function of Hfq-binding sRNAs by degrading target mRNA-derived fragments. [PDF]
Nucleic Acids Res, 2019 In many Gram-negative and some Gram-positive bacteria, small regulatory RNAs (sRNAs) that bind the RNA chaperone Hfq have a pivotal role in modulating virulence, stress responses, metabolism and biofilm formation.
Cameron TA, Matz LM, Sinha D, De Lay NR.
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Human polynucleotide phosphorylase in mitochondrial RNA metabolism. [PDF]
Biosci RepEver since its discovery more than 70 years ago, the enzyme polynucleotide phosphorylase (PNPase) has been the subject of intensive research that has highlighted its key functional roles.
Bakshi N +3 more
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RNA processing factor 7 and polynucleotide phosphorylase are necessary for processing and stability of nad2 mRNA in Arabidopsis mitochondria. [PDF]
RNA Biol, 2014 Stoll B, Zendler D, Binder S.
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Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: STRUCTURAL MAPPING AND EFFECT ON mRNA TURNOVER. [PDF]
J Biol Chem, 2016 Polynucleotide phosphorylase (PNPase), a 3′-to-5′ phosphorolytic exoribonuclease, is thought to be the primary enzyme responsible for turnover of Bacillus subtilis mRNA. The role of PNPase in B.
Salvo E +4 more
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Localization of components of the RNA-degrading machine in Bacillus subtilis [PDF]
Frontiers in Microbiology, 2016 In bacteria, the control of mRNA stability is crucial to allow rapid adaptation to changing conditions. In most bacteria, RNA degradation is catalyzed by the RNA degradosome, a protein complex composed of endo- and exoribonucleases, RNA helicases and ...
Nora Cascante-Estepa +2 more
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RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region. [PDF]
RNA, 2014 The endoribonuclease RNase E in a range of bacteria has a conserved N-terminal catalytic domain and a less well-conserved C-terminal tail. While the role of the C-terminal tail in the formation of the degradosome, including the interaction with the ...
Zhang JY +6 more
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Crystal structure of Caulobacter crescentus polynucleotide phosphorylase reveals a mechanism of RNA substrate channelling and RNA degradosome assembly [PDF]
Open Biology, 2012 Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3′–5′ directionality and processive behaviour.
Steven W. Hardwick +4 more
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Helicase SUV3, polynucleotide phosphorylase, and mitochondrial polyadenylation polymerase form a transient complex to modulate mitochondrial mRNA polyadenylated tail lengths in response to energetic changes. [PDF]
J Biol Chem, 2014 Background: Helicase SUV3, polynucleotide phosphorylase (PNPase), or mitochondrial poly(A) polymerases (mtPAP) have individual activity in regulating mitochondrial mRNA (mt-mRNA)-polyadenylated (poly(A)) tails.
Wang DD +5 more
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Exploring the mitochondrial microRNA import pathway through Polynucleotide Phosphorylase (PNPase). [PDF]
J Mol Cell Cardiol, 2017 Shepherd DL +9 more
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