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Polyribonucleotide nucleotidyltransferase 1

polynucleotide phosphorylase, Polyribonucleotide Nucleotidyltransferase
PNPT1 is a subunit of the exosome complex, which is involved in 3-prime-to-5-prime exoribonuclease activity for RNA processing and degradation (Raijmakers et al., 2002 [PubMed 12419256]).[supplied by OMIM, Mar 2008] (from NCBI)
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Top mentioned proteins: CAN, ACID, PNP, exoribonuclease, caspase-3
Papers on polynucleotide phosphorylase
The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes.
De Lay et al., Cambridge, United Kingdom. In Rna, Feb 2016
Many of the actions of these nucleic acids are mediated by well-characterized chaperones such as the Hfq protein, but genetic screens have also recently identified the 3'-to-5' exoribonuclease polynucleotide phosphorylase (PNPase) as an unexpected stabilizer and facilitator of sRNAs in vivo.
The hmsT 3' untranslated region mediates c-di-GMP metabolism and biofilm formation in Yersinia pestis.
Sun et al., Beijing, China. In Mol Microbiol, Jan 2016
We also found that polynucleotide phosphorylase is partially responsible for hmsT 3'UTR-mediated mRNA decay.
The Protein Interaction of RNA Helicase B (RhlB) and Polynucleotide Phosphorylase (PNPase) Contributes to the Homeostatic Control of Cysteine in Escherichia coli.
Lin-Chao et al., Taipei, Taiwan. In J Biol Chem, Jan 2016
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.
Direct observation of processive exoribonuclease motion using optical tweezers.
Block et al., Cambridge, United Kingdom. In Proc Natl Acad Sci U S A, Jan 2016
In Escherichia coli, the exoribonucleases RNase R and polynucleotide phosphorylase (PNPase) play critical roles in degrading RNA.
Killing of cancer cells through the use of eukaryotic expression vectors harbouring genes encoding nucleases and ribonuclease inhibitor.
Glinka, Moscow, Russia. In Tumour Biol, May 2015
This review is focused on vectors bearing genes for nucleases such as deoxyribonucleases (caspase-activated DNase, deoxyribonuclease I-like 3, endonuclease G) and ribonucleases (human polynucleotide phosphorylase, ribonuclease L, α-sarcin, barnase), as well as vectors harbouring gene encoding ribonuclease inhibitor.
Structure and function of the archaeal exosome.
Klug et al., Gießen, Germany. In Wiley Interdiscip Rev Rna, 2014
The RNA-degrading exosome in archaea is structurally very similar to the nine-subunit core of the essential eukaryotic exosome and to bacterial polynucleotide phosphorylase (PNPase).
Non-coding Y RNAs as tethers and gates: Insights from bacteria.
Wang et al., New Haven, United States. In Rna Biol, 2013
Although the function of Ro60 RNPs has been mysterious, we recently reported that a bacterial Y RNA tethers Ro60 to the 3' to 5' exoribonuclease polynucleotide phosphorylase (PNPase) to form RYPER (Ro60/Y RNA/PNPase Exoribonuclease RNP), a new RNA degradation machine.
An RNA degradation machine sculpted by Ro autoantigen and noncoding RNA.
Wolin et al., New Haven, United States. In Cell, 2013
We report that Rsr and the exoribonuclease polynucleotide phosphorylase (PNPase) form an RNA degradation machine that is scaffolded by Y RNA.
The exoribonuclease Polynucleotide Phosphorylase influences the virulence and stress responses of yersiniae and many other pathogens.
Chopra et al., Houston, United States. In Front Cell Infect Microbiol, 2012
The three pathogenic yersiniae (Yersinia pestis, Y. pseudo-tuberculosis, and Y. enterocolitica) are all psychrotropic bacteria capable of growth at 4°C; however, cold growth is dependent on the presence of an exoribonuclease, polynucleotide phosphorylase (PNPase).
Human polynucleotide phosphorylase (hPNPaseold-35): should I eat you or not--that is the question?
Fisher et al., Richmond, United States. In Adv Cancer Res, 2012
3'-5' exoribonucleases are essential mediators of RNA decay pathways, and one such evolutionarily conserved enzyme is polynucleotide phosphorylase (PNPase).
Nuclear EGFR suppresses ribonuclease activity of polynucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776.
Hung et al., Taiwan. In J Biol Chem, 2012
a novel role of nEGFR in radioresistance, and that is, upon ionizing radiation, nEGFR inactivates the ribonuclease activity of PNPase toward c-MYC mRNA through DNAPK-mediated Ser-776 phosphorylation
Crystal structure of human polynucleotide phosphorylase: insights into its domain function in RNA binding and degradation.
Yuan et al., Taiwan. In Nucleic Acids Res, 2012
The study provides structural and functional insights into hPNPase, which uses a KH pore to trap a long RNA 3' tail that is further delivered into an RNase PH channel for the degradation process.
Involvement of pnp in survival of UV radiation in Escherichia coli K-12.
Jawali et al., Mumbai, India. In Microbiology, 2012
Absence of PNPase decreases the survival of cells exposed to UV radiation.
Role of polynucleotide phosphorylase in sRNA function in Escherichia coli.
Gottesman et al., Bethesda, United States. In Rna, 2011
Role of polynucleotide phosphorylase in sRNA function in Escherichia coli
Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli.
Luisi et al., Cambridge, United Kingdom. In J Biol Chem, 2011
Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli
Mitochondrial matrix reloaded with RNA.
Yoshihisa et al., Nagoya, Japan. In Cell, 2010
Wang et al. (2010) now find that polynucleotide phosphorylase in the intermembrane space of mammalian mitochondria facilitates import of several RNAs into the mitochondrial matrix.
PNPASE regulates RNA import into mitochondria.
Teitell et al., Los Angeles, United States. In Cell, 2010
The data support an unanticipated role for PNPASE in mediating the translocation of RNAs into mitochondria
Exoribonucleases and Endoribonucleases.
Deutscher et al., In Ecosal Plus, 2004
These are RNases II, R, D, T, PH, BN, polynucleotide phosphorylase (PNPase), and oligoribonuclease (ORNase).
DOTY et al., In Science, 1965
Conditions have been found under which polynucleotide phosphorylase adds only a few nucleotide residues to the 3' end of a dinucleotide primer.
DOTY et al., In Science, 1965
The concentration of sodium chloride strongly influences primed polymerization of nucleoside diphosphates by polynucleotide phosphorylase.
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