Structural insights into the dimeric human PNPase revealing why the disease-linked mutants exhibit lower RNA import and degradation activities [PDF]
Acta Crystallographica Section A: Foundations and Advances, 2018 Polynucleotide phosphorylase (PNPase) is an evolutionary conserved 3'-to-5' exoribonuclease that functions differently among species, ranging from RNA turnover in bacteria to RNA transport in mammals.
B. Golzarroshan +3 more
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Purine nucleoside phosphorylase as a target for the treatment of interstitial cystitis/bladder pain syndrome with and without Hunner lesions [PDF]
Scientific ReportsChronic visceral pain disorders, such as interstitial cystitis/bladder pain syndrome (IC/BPS), are difficult to treat, and therapies are limited in number and efficacy.
Lori A. Birder +6 more
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Human mitochondrial RNA decay mediated by PNPase–hSuv3 complex takes place in distinct foci [PDF]
Nucleic Acids Research, 2012 RNA decay is usually mediated by protein complexes and can occur in specific foci such as P-bodies in the cytoplasm of eukaryotes. In human mitochondria nothing is known about the spatial organization of the RNA decay machinery, and the ribonuclease responsible for RNA degradation has not been identified.
Lukasz S. Borowski +4 more
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Selective RNA Processing and Stabilization are Multi‐Layer and Stoichiometric Regulators of Gene Expression in Escherichia coli [PDF]
Advanced Science, 2023 Selective RNA processing and stabilization (SRPS) facilitates the differential expression of multiple genes in polycistronic operons. However, how the coordinated actions of SRPS‐related enzymes affect stoichiometric regulation remains unclear.
Daixi Liu +5 more
doaj +2 more sources
Journal of Biological Chemistry, 2015 PNPase, one of the major enzymes with 3′ to 5′ single-stranded RNA degradation and processing activities, can interact with the RNA helicase RhlB independently of RNA degradosome formation in Escherichia coli.
Y. Tseng +3 more
semanticscholar +2 more sources
PNPase is a key player in the regulation of small RNAs that control the expression of outer membrane proteins [PDF]
RNA, 2008 In this report, we demonstrate that exonucleolytic turnover is much more important in the regulation of sRNA levels than was previously recognized. For the first time, PNPase is introduced as a major regulatory feature controlling the levels of the small noncoding RNAs MicA and RybB, which are required for the accurate expression of outer membrane ...
José M. Andrade, Cecília M. Arraiano
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Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation [PDF]
RNA, 2008 Bacterial polynucleotide phosphorylase (PNPase) plays a major role in mRNA turnover by the degradation of RNA from the 3′- to 5′-ends. Here, we determined the crystal structures of the wild-type and a C-terminal KH/S1 domain-truncated mutant (ΔKH/S1) of Escherichia coli PNPase at resolutions of 2.6 Å and 2.8 Å, respectively. The six RNase PH domains of
Zhonghao Shi +4 more
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Rapid and scalable detection of synthetic mRNA byproducts using polynucleotide phosphorylase and polythymidine oligonucleotides [PDF]
RNA BiologyProduction and storage of synthetic mRNA can introduce a variety of byproducts which reduce the overall integrity and functionality of mRNA vaccines and therapeutics.
Francis Combes +3 more
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A Mutation in PNPT1, Encoding Mitochondrial-RNA-Import Protein PNPase, Causes Hereditary Hearing Loss [PDF]
The American Journal of Human Genetics, 2012 A subset of nuclear-encoded RNAs has to be imported into mitochondria for the proper replication and transcription of the mitochondrial genome and, hence, for proper mitochondrial function. Polynucleotide phosphorylase (PNPase or PNPT1) is one of the very few components known to be involved in this poorly characterized process in mammals.
Simon von Ameln +23 more
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Phenotypic Characterization of PNPase Mutation and Overexpression in C. elegans [PDF]
, 2019 PNPase, polynucleotide phosphorylase, is a multifunctional exoribonuclease protein with 3` terminal oligonucleotide polymerase activity. Coded by the PNPT1 gene, the protein is associated with mitochondrial homeostasis and functions as a possible target ...
Hur, Brian J
core +5 more sources