Results 11 to 20 of about 4,319 (202)

A PNPase dependent CRISPR System in Listeria. [PDF]

open access: yesPLoS Genetics, 2014
The human bacterial pathogen Listeria monocytogenes is emerging as a model organism to study RNA-mediated regulation in pathogenic bacteria. A class of non-coding RNAs called CRISPRs (clustered regularly interspaced short palindromic repeats) has been ...
Nina Sesto   +9 more
doaj   +7 more sources

Regulatory Mechanisms of Exoribonuclease PNPase and Regulatory Small RNA on T3SS of Dickeya dadantii [PDF]

open access: yesMolecular 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
doaj   +3 more sources

Human PNPase causes RNA stabilization and accumulation of R-loops in the Escherichia coli model system

open access: yesScientific Reports, 2023
Polyribonucleotide phosphorylase (PNPase) is a phosphorolytic RNA exonuclease highly conserved throughout evolution. In Escherichia coli, PNPase controls complex phenotypic traits like biofilm formation and growth at low temperature.
Federica A. Falchi   +7 more
doaj   +4 more sources

PNPase knockout results in mtDNA loss and an altered metabolic gene expression program.

open access: yesPLoS ONE, 2018
Polynucleotide phosphorylase (PNPase) is an essential mitochondria-localized exoribonuclease implicated in multiple biological processes and human disorders.
Eriko Shimada   +11 more
doaj   +6 more sources

Lack of PNPase activity in Enterococcus faecalis 14 increases the stability of EntDD14 bacteriocin transcripts

open access: yesScientific Reports, 2023
A mutant deficient in polynucleotide phosphorylase (PNPase) activity was previously constructed in Enterococcus faecalis 14; a strain producing a leaderless two-peptide enterocin DD14 (EntDD14).
Rabia Ladjouzi   +3 more
doaj   +5 more sources

Single-exonuclease nanocircuits reveal the RNA degradation dynamics of PNPase and demonstrate potential for RNA sequencing

open access: yesNature Communications, 2023
Observing the natural process of RNA degradation in real-time is a significant challenge. Here, the authors develop and use single-exonuclease nanocircuits to reveal the single-base degradation behaviour of PNPase, and demonstrate proof-of-principle RNA ...
Zhiheng Yang   +6 more
doaj   +3 more sources

The small RNA SraG participates in PNPase homeostasis [PDF]

open access: yesRNA, 2016
The rpsO-pnp operon encodes ribosomal protein S15 and polynucleotide phosphorylase, a major 3′–5′ exoribonuclease involved in mRNA decay in Escherichia coli. The gene for the SraG small RNA is located between the coding regions of the rpsO and pnp genes, and it is transcribed in the opposite direction relative to the two genes.
Fontaine, Fanette   +6 more
  +9 more sources

Structural insights into human PNPase in health and disease. [PDF]

open access: yesNucleic Acids Res
Abstract Human polynucleotide phosphorylase (hPNPase) is a 3′-to-5′ exoribonuclease located in mitochondria, where it plays crucial roles in RNA degradation and RNA import. Mutations in hPNPase can impair these functions, leading to various mitochondrial dysfunctions and diseases. However, the mechanisms by which hPNPase switches between
Li YC   +5 more
europepmc   +3 more sources

A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation [PDF]

open access: yesMolecular Cell, 2020
Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic ...
Tom Dendooven   +6 more
openaire   +2 more sources

Unconventional mRNA processing and degradation pathways for the polycistronic yrzI (spyTA) mRNA in Bacillus subtilis. [PDF]

open access: yesFEBS Lett
The S1025 peptide is the major antidote to the YrzI toxin, which we renamed here as SpyT (Small Peptide YrzI Toxin) and SpyA (Small Peptide YrzI Antitoxin) (1). Degradation of the toxin–antitoxin spyTA mRNA, either by a translation‐dependent cleavage by the endoribonuclease Rae1 (2) or by direct attack by 3′‐exoribonucleases (3), also contributes to ...
Gilet L   +4 more
europepmc   +2 more sources

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