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Information on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8TCS8

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IUBMB Comments
ADP, IDP, GDP, UDP and CDP can act as donors.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q8TCS8
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
AtcpPNPase, AtmtPNPase, chloroplast PNPase, cpPNPase, hPNPase(old-35), hPNPaseold-35, nucleoside diphosphate:polynucleotidyl transferase, nucleotidyltransferase, polyribonucleotide, PNP, PNPase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hPNPase(old-35)
247
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hPNPaseold-35
247
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nucleoside diphosphate:polynucleotidyl transferase
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nucleotidyltransferase, polyribonucleotide
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PNPase
polynucleotide phosphorylase
polyribonucleotide phosphorylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RNAn+1 + phosphate = RNAn + a nucleoside diphosphate
show the reaction diagram
mechanism of elongation, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
polyribonucleotide:phosphate nucleotidyltransferase
ADP, IDP, GDP, UDP and CDP can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-12-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
24-nucleotide RNA molecule + ADP
25-nucleotide RNA molecule + phosphate
show the reaction diagram
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when both ADP and phosphate are present at the reaction mixture, the direction of activity, either polyadenylation or degradation, is dependent on their relative concentrations
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r
24-nucleotide RNA molecule + phosphate
23-nucleotide RNA molecule + nucleoside diphosphate
show the reaction diagram
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when both ADP and phosphate are present at the reaction mixture, the direction of activity, either polyadenylation or degradation, is dependent on their relative concentrations
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r
microR-221 RNAn+1 + phosphate
microR-221 RNAn + ADP
show the reaction diagram
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recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184 as substrates, the recombinant enzyme selectively and preferentially degrades microRNA-221 in human melanoma cells
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r
microRNAn+1 + phosphate
microRNAn + ADP
show the reaction diagram
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recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184
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r
poly(A) + ADP
poly(A)+1 + phosphate
show the reaction diagram
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-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
show the reaction diagram
-
specificity overview
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r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + ADP
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + ADP
show the reaction diagram
G8TCS8
the enzyme catalyzes the processive phosphorolysis of RNA by using an inorganic phosphate to cleave the phosphodiester linkage at the 3'-end of a RNA chain
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-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydrogen peroxide
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upon exposure of human cells, the amount of enzyme protein decreases rapidly
menadione
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upon exposure of human cells, the amount of enzyme protein decreases rapidly
phosphate
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inhibitory at about 10 mM
additional information
-
no specific decrease in enzyme protein level upon treatment of cells with cycloheximide or ACNU, i.e. 1-(4-amino-2-methyl-5-pyrimidinyl) methyl-3-(2-chloroethyl)-3-nitrosurea hydrochloride
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
interferon-beta
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close association between interferon-beta induced upregulation of enzyme and c-myc downregulation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
enzyme binding with RNA displays an apparent sigmoid curve, with a Kd of 16 nM
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
pre-B cell
Manually annotated by BRENDA team
additional information
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enzyme expression level analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
structure of the S1 pore in exosomes and the KH pore in hPNPase, overview
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Manually annotated by BRENDA team
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localizes to the intermembrane space of mitochondria as a peripheral membrane protein in a multimeric complex
Manually annotated by BRENDA team
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HeLa cells
Manually annotated by BRENDA team
additional information
KH pore in PNPase versus S1 pore in exosomes
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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human polynucleotide phosphorylase is an evolutionary conserved RNA-processing enzyme. PNPase contains five motifs that are conspicuously preserved through evolution extending from prokaryotes and plants to mammals. Although hPNPase structurally and biochemically resembles PNPase of other species, overexpression and inhibition studies reveal that hPNPase has evolved to serve more specialized and diversified functions in humans
malfunction
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inhibition of the enzyme by shRNA or stable overexpression of miR-221 protects melanoma cells from IFN-beta-mediated growth inhibition
metabolism
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the enzyme is involved in RNA degradation and/turnover, major processes controlling RNA levels and important regulators of physiological and pathological processes
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PNPT1_HUMAN
783
0
85951
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80900
3 * 80900, about, sequence calculation, the trimeric hPNPase has a hexameric ring-like structure formed by six RNase PH domains, capped with a trimeric KH pore, the enzyme has a conserved GXXG motif in the KH domain, structural model of hPNPase, overview
90000
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3 * 90000, SDS-PAGe and homology modeling
207600
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equilibrium sedimentation analytical ultracentrifugation
230000
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gel filtration
240000
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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processing of the N-terminal targeting sequence upon import into mitochondria
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
homology modeling based on structure of Streptomyces antibioticus ortholog. Enzyme displays a doughnut-shaped trimer with a central channel to accommodate a single-stranded RNA molecule. The circular structure is composed of the first and second core domains, while the KH and S1 RNA binding domains are located at the top, adjacent to the gate entrance into the circle
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wild-type and S1 domain-truncated hPNPase, hanging-drop vapor diffusion method, mixxing of 0.001 ml of 10 mg/ml protein in 50 mM Tris, pH 8.0, and 150 mM NaCl, with 0.001 ml of reservoir solution containing 0.1 M citrate, pH 5.0, 10% v/v 2-propanol and 26% v/v PEG 400, room temperature, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D135G
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unlike trimeric wild-type, mutant is monomeric. Almost complete inhibition of degradation and polyadenylation activities
D544G
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decrease in degradation activity, increase in polymerization
G622D
site-directed mutagenesis
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
MonoQ colmn chromatography, metal ion affinity chromatography, and Superdex 200 gel filtration
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recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by nickel affinty chromatography and gel filtration
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
ectopic expression of human polynucleotide phosphorylase, i.e. hPNPaseold-35, in human HO-1 melanoma cells results in growth suppression
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enhanced expression of hPNPase(old-35) via a replication-incompetent adenovirus (Ad.hPNPase(old-35)) in human melanoma cells and normal melanocytes
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expressed in Escherichia coli Rosetta cells
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expression in HeLa cell
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expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL
gene cloning using an overlapping pathway screening strategy designed to identify genes coordinately regulated during the processes of cellular differentiation and senescence, overview. Expression in HO-1 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
molecular biology
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targeted overexpression of hPNPase represents a strategy to selectively downregulate RNA expression and consequently intervene in a variety of pathophysiological conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Godefroy-Colburn, T.; Grunenberg-Manago, M.
Polynucleotide phosphorylase
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
7
533-574
1972
Ascaris lumbricoides, Auxenochlorella pyrenoidosa, Cavia porcellus, Escherichia coli, Halobacterium salinarum, Homo sapiens, Lactobacillus plantarum, Micrococcus luteus, Neisseria meningitidis, Pseudomonas aeruginosa, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Spinacia oleracea, Synechococcus elongatus PCC 7942, Triticum aestivum
-
Manually annotated by BRENDA team
Leszczyniecka, M.; Kang, D.C.; Sarkar, D.; Su, Z.Z.; Holmes, M.; Valerie, K.; Fisher, P.B.
Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence
Proc. Natl. Acad. Sci. USA
99
16636-16641
2002
Homo sapiens, Homo sapiens (Q8TCS8)
Manually annotated by BRENDA team
Sarkar, D.; Lebedeva, I.V.; Emdad, L.; Kang, D.C.; Baldwin, A.S.; Fisher, P.B.
Human polynucleotide phosphorylase (hPNPaseold-35): a potential link between aging and inflammation
Cancer Res.
64
7473-7478
2004
Homo sapiens
Manually annotated by BRENDA team
Nagaike, T.; Suzuki, T.; Katoh, T.; Ueda, T.
Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase
J. Biol. Chem.
280
19721-19727
2005
Homo sapiens
Manually annotated by BRENDA team
Hayakawa, H.; Sekiguchi, M.
Human polynucleotide phosphorylase protein in response to oxidative stress
Biochemistry
45
6749-6755
2006
Homo sapiens
Manually annotated by BRENDA team
French, S.W.; Dawson, D.W.; Chen, H.; Rainey, R.N.; Sievers, S.A.; Balatoni, C.E.; Wong, L.; Troke, J.J.; Nguyen, M.T.; Koehler, C.M.; Teitell, M.A.
The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity
Cancer Lett.
248
198-210
2007
Homo sapiens (Q8TCS8)
Manually annotated by BRENDA team
Sarkar, D.; Park, E.S.; Fisher, P.B.
Defining the mechanism by which IFN-beta dowregulates c-myc expression in human melanoma cells: pivotal role for human polynucleotide phosphorylase (hPNPaseold-35)
Cell Death Differ.
13
1541-1553
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, H.W.; Rainey, R.N.; Balatoni, C.E.; Dawson, D.W.; Troke, J.J.; Wasiak, S.; Hong, J.S.; McBride, H.M.; Koehler, C.M.; Teitell, M.A.; French, S.W.
Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis
Mol. Cell. Biol.
26
8475-8487
2006
Homo sapiens
Manually annotated by BRENDA team
Wu, J.; Li, Z.
Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress
Biochem. Biophys. Res. Commun.
372
288-292
2008
Homo sapiens
Manually annotated by BRENDA team
Sarkar, D.; Park, E.S.; Barber, G.N.; Fisher, P.B.
Activation of double-stranded RNA dependent protein kinase, a new pathway by which human polynucleotide phosphorylase (hPNPase(old-35)) induces apoptosis
Cancer Res.
67
7948-7953
2007
Homo sapiens
Manually annotated by BRENDA team
Chan, I.; Lebedeva, I.V.; Su, Z.Z.; Sarkar, D.; Valerie, K.; Fisher, P.B.
Progression elevated gene-3 promoter (PEG-Prom) confers cancer cell selectivity to human polynucleotide phosphorylase (hPNPase(old-35))-mediated growth suppression
J. Cell. Physiol.
215
401-409
2008
Homo sapiens
Manually annotated by BRENDA team
Portnoy, V.; Palnizky, G.; Yehudai-Resheff, S.; Glaser, F.; Schuster, G.
Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts
RNA
14
297-309
2008
Homo sapiens
Manually annotated by BRENDA team
Slomovic, S.; Schuster, G.
Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA
RNA
14
310-323
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, D.D.; Shu, Z.; Lieser, S.A.; Chen, P.L.; Lee, W.H.
Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality
J. Biol. Chem.
284
20812-20821
2009
Homo sapiens
Manually annotated by BRENDA team
Lin, C.L.; Wang, Y.T.; Yang, W.Z.; Hsiao, Y.Y.; Yuan, H.S.
Crystal structure of human polynucleotide phosphorylase: insights into its domain function in RNA binding and degradation
Nucleic Acids Res.
40
4146-4157
2012
Homo sapiens (G8TCS8), Homo sapiens
Manually annotated by BRENDA team
Das, S.K.; Bhutia, S.K.; Sokhi, U.K.; Dash, R.; Azab, B.; Sarkar, D.; Fisher, P.B.
Human polynucleotide phosphorylase (hPNPase(old-35)): an evolutionary conserved gene with an expanding repertoire of RNA degradation functions
Oncogene
30
1733-1743
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Das, S.K.; Sokhi, U.K.; Bhutia, S.K.; Azab, B.; Su, Z.Z.; Sarkar, D.; Fisher, P.B.
Human polynucleotide phosphorylase selectively and preferentially degrades microRNA-221 in human melanoma cells
Proc. Natl. Acad. Sci. USA
107
11948-11953
2010
Homo sapiens
Manually annotated by BRENDA team
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