Identification of genes potentially regulated by human polynucleotide phosphorylase (hPNPase old-35) using melanoma as a model. [PDF]
Human Polynucleotide Phosphorylase (hPNPase(old-35) or PNPT1) is an evolutionarily conserved 3'→ 5' exoribonuclease implicated in the regulation of numerous physiological processes including maintenance of mitochondrial homeostasis, mtRNA import and ...
Upneet K Sokhi +8 more
doaj +3 more sources
Regulation of Escherichia coli Polynucleotide Phosphorylase by ATP [PDF]
Polynucleotide phosphorylase (PNPase), an enzyme conserved in bacteria and eukaryotic organelles, processively catalyzes the phosphorolysis of RNA, releasing nucleotide diphosphates, and the reverse polymerization reaction. In Escherichia coli, both reactions are implicated in RNA decay, as addition of either poly(A) or heteropolymeric tails targets ...
M. Del Favero +5 more
core +8 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 +2 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 +2 more sources
Oocyte Factors Suppress Mitochondrial Polynucleotide Phosphorylase to Remodel the Metabolome and Enhance Reprogramming [PDF]
Oocyte factors not only drive somatic cell nuclear transfer reprogramming but also augment the efficiency and quality of induced pluripotent stem cell (iPSC) reprogramming.
Swea-Ling Khaw +4 more
doaj +2 more sources
Activity and Function in Human Cells of the Evolutionary Conserved Exonuclease Polynucleotide Phosphorylase. [PDF]
Polynucleotide phosphorylase (PNPase) is a phosphorolytic RNA exonuclease highly conserved throughout evolution. Human PNPase (hPNPase) is located in mitochondria and is essential for mitochondrial function and homeostasis. Not surprisingly, mutations in
Falchi FA, Pizzoccheri R, Briani F.
europepmc +2 more sources
Streptomyces RNases – Function and impact on antibiotic synthesis
Streptomyces are soil dwelling bacteria that are notable for their ability to sporulate and to produce antibiotics and other secondary metabolites. Antibiotic biosynthesis is controlled by a variety of complex regulatory networks, involving activators ...
George H. Jones
doaj +1 more source
Neisseria meningitidis Polynucleotide Phosphorylase Affects Aggregation, Adhesion, and Virulence. [PDF]
Neisseria meningitidis autoaggregation is an important step during attachment to human cells. Aggregation is mediated by type IV pili and can be modulated by accessory pilus proteins, such as PilX, and posttranslational modifications of the major pilus ...
Engman J +8 more
europepmc +2 more sources
The discovery of the mechanisms of biological synthesis of nucleic acids: 1959 Nobel laureates S. Ochoa and A. Kornberg [PDF]
Alongside the chemical and physical research of nucleic acids in the 1940s-50s, the mechanisms of their biosynthesis were investigated. Thus, in 1959, Severo Ochoa and Arthur Kornberg were awarded the Nobel Prize in Physiology or Medicine for the ...
O. P. Matyshevska +2 more
doaj +1 more source
Regulation of miRNA content. Part 2. Degradation of miRNAs
The scientific review presents the process of regulation of microRNA content — microRNA degradation. To write the article, information was searched using databases Scopus, Web of Science, MedLine, PubMed, Google Scholar, EMBASE, Global Health, The ...
A.E. Abaturov, V.L. Babуch
doaj +1 more source

