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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Phenotypic Characterization of PNPase Mutation and Overexpression in C. elegans
, 2019 VCU Theses and ...
Brian J Hur
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Identification of Polynucleotide Phosphorylase (PNPase) in Escherichia coli Involved in Persister Formation [PDF]
bioRxiv, 2018 Despite the identification of many genes and pathways involved in the persistence phenomenon of bacteria, the mechanisms of persistence are not well understood.
Nan Wu +9 more
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Unconventional mRNA processing and degradation pathways for the polycistronic yrzI (spyTA) mRNA in Bacillus subtilis. [PDF]
FEBS LettThe 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
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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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Modular domain organization of RNase E and PNPase
, 2009 mRNA decay in Escherichia coli is carried out and controlled by concerted actions of a number of ribonucleases and other protein factors. In order to gain insights into the catalytic mechanisms and regulation involved in this important cellular process, we have utilized mutational analysis to study two key enzymes, RNase E and PNPase.
Xin Miao
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Polynucleotide phosphorylase: Not merely an RNase but a pivotal post-transcriptional regulator. [PDF]
PLoS Genetics, 2018 Almost 60 years ago, Severo Ochoa was awarded the Nobel Prize in Physiology or Medicine for his discovery of the enzymatic synthesis of RNA by polynucleotide phosphorylase (PNPase).
Todd A Cameron +2 more
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Isolate Specific Cold Response of Yersinia enterocolitica in Transcriptional, Proteomic, and Membrane Physiological Changes [PDF]
, 2020 Yersinia enterocolitica, a zoonotic foodborne pathogen, is able to withstand low temperatures. This psychrotrophic ability allows it to multiply in food stored in refrigerators. However, little is known about the Y. enterocolitica cold response.
Alter, Thomas +4 more
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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.
Yi-Ting Tseng +3 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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