Polynucleotide phosphorylase and RNA helicase CshA cooperate in Bacillus subtilis mRNA decay. [PDF]
Polynucleotide phosphorylase (PNPase), a 3ʹ exoribonuclease that degrades RNA in the 3ʹ-to-5ʹ direction, is the major mRNA decay activity in Bacillus subtilis.
Ingle S +5 more
europepmc +4 more sources
Polynucleotide phosphorylase is implicated in homologous recombination and DNA repair in Escherichia coli [PDF]
Background Polynucleotide phosphorylase (PNPase, encoded by pnp) is generally thought of as an enzyme dedicated to RNA metabolism. The pleiotropic effects of PNPase deficiency is imputed to altered processing and turnover of mRNAs and small RNAs, which ...
Thomas Carzaniga +3 more
doaj +3 more sources
Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7 [PDF]
Polynucleotide phosphorylase (PNPase) is reported to regulate virulence in Salmonella, Yersinia spp. and Campylobacter jejuni, yet its role in Escherichia coli O157:H7 has not been investigated. To gain insights into its roles in E.
Jia eHu, Jia eHu, Meijun eZhu
doaj +3 more sources
Human polynucleotide phosphorylase in mitochondrial RNA metabolism. [PDF]
Ever 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
europepmc +4 more sources
Polynucleotide phosphorylase regulates multiple virulence factors and the stabilities of small RNAs RsmY/Z in Pseudomonas aeruginosa [PDF]
Post-transcriptional regulation enables bacteria to quickly response to environmental stresses. Polynucleotide phosphorylase (PNPase), which contains an N-terminal catalytic core and C-terminal RNA binding KH-S1 domains, is involved in RNA processing ...
Ronghao eChen +10 more
doaj +3 more sources
Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: STRUCTURAL MAPPING AND EFFECT ON mRNA TURNOVER. [PDF]
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
europepmc +4 more sources
The Protein Interaction of RNA Helicase B (RhlB) and Polynucleotide Phosphorylase (PNPase) Contributes to the Homeostatic Control of Cysteine in Escherichia coli. [PDF]
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.
Tseng YT +3 more
europepmc +3 more sources
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]
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
europepmc +4 more sources
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region. [PDF]
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
europepmc +4 more sources
The exoribonuclease Polynucleotide Phosphorylase influences the virulence and stress responses of yersiniae and many other pathogens [PDF]
Microbes are incessantly challenged by both biotic and abiotic stressors threatening their existence. Therefore, bacterial pathogens must possess mechanisms to successfully subvert host immune defenses as well as overcome the stress associated with host ...
Jason A. Rosenzweig, Ashok K Chopra
doaj +3 more sources

