Polynucleotide phosphorylase has an impact on cell biology of Campylobacter jejuni [PDF]
Frontiers 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
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Rapid Degradation of Hfq-Free RyhB in Yersinia pestis by PNPase Independent of Putative Ribonucleolytic Complexes [PDF]
BioMed Research International, 2014 The RNA chaperone Hfq in bacteria stabilizes sRNAs by protecting them from the attack of ribonucleases. Upon release from Hfq, sRNAs are preferably degraded by PNPase. PNPase usually forms multienzyme ribonucleolytic complexes with endoribonuclease E and/
Zhongliang Deng +6 more
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PNPASE and RNA trafficking into mitochondria [PDF]
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2011 The mitochondrial genome encodes a very small fraction of the macromolecular components that are required to generate functional mitochondria. Therefore, most components are encoded within the nuclear genome and are imported into mitochondria from the cytosol.
Geng Wang +3 more
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Ring around the Ro-sie: RNA-Mediated Alterations of PNPase Activity [PDF]
Cell, 2013 Chen et al. demonstrate a new way by which noncoding RNAs tailor the function of multicomponent complexes. They show that a noncoding RNA interacts with an exoribonuclease, altering its substrate specificity and enzymatic activity by serving as a ribonucleoprotein scaffold and, perhaps, a gate for entry of the RNA substrate.
Brian J. Geiss, Jeffrey Wilusz
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PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader [PDF]
The EMBO Journal, 2001 Polynucleotide phosphorylase synthesis is autocontrolled at a post-transcriptional level in an RNase III-dependent mechanism. RNase III cleaves a long stem-loop in the pnp leader, which triggers pnp mRNA instability, resulting in a decrease in the synthesis of polynucleotide phosphorylase.
A.-C. Jarrige
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Exploring the mitochondrial microRNA import pathway through Polynucleotide Phosphorylase (PNPase). [PDF]
Journal of Molecular and Cellular Cardiology, 2017 Cardiovascular disease is the primary cause of mortality for individuals with type 2 diabetes mellitus. During the diabetic condition, cardiovascular dysfunction can be partially attributed to molecular changes in the tissue, including alterations in microRNA (miRNA) interactions.
D. Shepherd +9 more
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Stable PNPase RNAi silencing: Its effect on the processing and adenylation of human mitochondrial RNA [PDF]
RNA, 2007 Polynucleotide phosphorylase (PNPase) is a diverse enzyme, involved in RNA polyadenylation, degradation, and processing in prokaryotes and organelles. However, in human mitochondria, PNPase is located in the intermembrane space (IMS), where no mitochondrial RNA (mtRNA) is known to be present.
Shimyn Slomovic, Gadi Schuster
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The crucial role of PNPase in the degradation of small RNAs that are not associated with Hfq [PDF]
RNA, 2012 The transient existence of small RNAs free of binding to the RNA chaperone Hfq is part of the normal dynamic lifecycle of a sRNA. Small RNAs are extremely labile when not associated with Hfq, but the mechanism by which Hfq stabilizes sRNAs has been elusive.
José M. Andrade +3 more
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Regulatory Mechanisms of Exoribonuclease PNPase and Regulatory Small RNA on T3SS of Dickeya dadantii [PDF]
Molecular Plant-Microbe Interactions, 2010 The type III secretion system (T3SS) is an essential virulence factor for many bacterial pathogens. Polynucleotide phosphorylase (PNPase) is one of the major exoribonucleases in bacteria and plays important roles in mRNA degradation, tRNA processing, and
Quan Zeng +3 more
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Target recognition by RNase E RNA-binding domain AR2 drives sRNA decay in the absence of PNPase
Proceedings of the National Academy of Sciences, 2022 Significance RNase E performs an indispensable function in gram-negative bacteria by initiating breakdown of cellular RNAs and providing the scaffold for the primary RNA decay machine, the RNA degradosome.
Dhriti Sinha, Nicholas R. De Lay
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