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Information on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase and Organism(s) Escherichia coli and UniProt Accession P05055

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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:
Escherichia coli
UNIPROT: P05055
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Escherichia coli
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
nucleoside diphosphate:polynucleotidyl transferase
-
-
-
-
nucleotidyltransferase, polyribonucleotide
-
-
-
-
PNPase
polynucleotide phosphorylase
polyribonucleotide phosphorylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RNAn+1 + phosphate = RNAn + a nucleoside diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
poly(A) + ADP
poly(A)+1 + phosphate
show the reaction diagram
poly(A)+1 + phosphate
poly(A) + ADP
show the reaction diagram
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
show the reaction diagram
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
show the reaction diagram
poly(I) + IDP
poly(I)+1 + phosphate
show the reaction diagram
rabbit globin mRNAn+1 + phosphate
ADP + rabbit globin mRNAn
show the reaction diagram
-
only the poly(A) tail of the mRNA is removed
-
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
show the reaction diagram
-
-
exchange reaction
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + ADP
show the reaction diagram
-
substrates used for the forward degradation reaction are poly(rA) 15-mer RNA and phosphate
substrates used for the reverse polymerization reaction are poly(rA) 15-mer RNA and ADP
-
r
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 + a nucleoside diphosphate
RNAn+1 + phosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme
Cd2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-Fluorouridine diphosphate
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-
6-azauridine
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Acridine orange
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-
ATP
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5 mM, 28°C, presence of MgCl2, 30% residual activity. Allosteric inhibition of both polymerization and phosphorolytic activities, mixed-type inhibition toward phosphate
beta,gamma-Imido-ATP
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5 mM, 28°C, presence of MgCl2, 50% residual activity
citrate
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a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. PNPase-dependent cells show reduced growth in the presence of increased citrate concentration. In vitro, citrate directly binds and modulates PNPase activity, and the enzyme is inhibited by binding of metal-chelated citrate, predominantly complexed as magnesium-citrate, in the active site at physiological concentrations. In the contrary, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity
dATP
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5 mM, 28°C, presence of MgCl2, 39% residual activity
dGTP
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5 mM, 28°C, presence of MgCl2, 40% residual activity
GTP
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5 mM, 28°C, presence of MgCl2, 65% residual activity
phosphonic acid analog of ADP
-
-
additional information
-
not inhibitory: CTP, UTP
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citrate
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a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. PNPase-dependent cells show reduced growth in the presence of increased citrate concentration. In vitro, citrate directly binds and modulates PNPase activity, and the enzyme is inhibited by binding of metal-chelated citrate, predominantly complexed as magnesium-citrate, in the active site at physiological concentrations. In the contrary, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity, this vestigial site as an allosteric binding pocket that recognizes metal-free citrate
diphosphate
-
activation of PNPase RNA synthesis activity at very low concentrations of phosphate
phosphate
spermidine
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0.1-1.0 mM, activates ADP-phosphate exchange 2fold
spermine
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0.1-1.0 mM, activates ADP-phosphate exchange 2fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000166
globin mRNA
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pH 8.0, 37°C, phosphorolysis of poly(A)tail from rabbit globin mRNA
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0.05
Mg2+
-
-
additional information
additional information
-
values for Km with polynucleotides longer than 20 nucleotides are much smaller than the Km for oligonucleotides which lies at approx. 0.05 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
recombinant enzyme activity is measured as repression of beta-galactosidase activity in the reporter expression sytem, RNA binding affinity and in vitro RNA-binding activities of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
8 - 9.5
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8
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assay at, forward degradation reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
45 - 55
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polymerization of UDP and CDP
60
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polymerization of ADP and GDP, phosphorolysis of poly A
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
intracellular levels of PNPase are regulated by polyadenylation levels of transcripts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
membrane vesicles
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
polynucleotide phosphorylase is a conserved, widely distributed phosphorolytic 3'-5' exoribonuclease
malfunction
metabolism
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
alpha3,beta2 or alpha3,betan, x * 86000 + x * 48000, enzyme form B is obtained by keeping the ionic strength at 200 mM during purification on Sephadex G-200, at lower salt concentrations the beta subunit tends to dissociate and the enzyme reverts to the A form
86000
100000
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low molecular weight form catalyzing phosphorolysis but unable to catalyze the polymerization of NDP's, can only phosphorolyze short-chain polymers and requires higher Mg2+ ion concentration
200000
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this form requires Mn2+ for NDP polymerization and has a higher Km for poly(A) phosphorolysis
230000
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ultracentrifugation, equilibrium sedimentaion analysis
252000
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enzyme form A
365000
-
enzyme form B
additional information
-
PNPase, the endoribonuclease RNase E, a DEAD-RNA helicase and the glycolytic enzyme enolase are associated with a high molecular weight complex, the degradosome
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
alpha3,beta2 or alpha3,betan, x * 86000 + x * 48000, enzyme form B is obtained by keeping the ionic strength at 200 mM during purification on Sephadex G-200, at lower salt concentrations the beta subunit tends to dissociate and the enzyme reverts to the A form
homotrimer
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monomer
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domain organization of the enzyme monomer, homology modeling with KH domain and S1 domain, overview
trimer
additional information
-
enzyme domains within residues 158-262 and 473-577 contain interaction sites for RNase E within a betabetaalphabetabetaalpha domain configuration
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
three-dimensional modeling of enzyme based on Streptomyces antibioticus protein structure. The binding domain for RNase E is located on the monomer surface, facing outward from the trimeric tertiary structure
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PNPase complexed with the recognition site from RNase E and with manganese in the presence or in the absence of modified RNA, hanging droplet vapor diffusion method, crystals for the PNPase core/RNase E micro-domain crystals are grown using 0.2 M ammonium nitrate, and 20% (w/v) PEG 3350, crystals for the PNPase core/RNase E microdomain-RNA complex are produced using 0.2 M diammonium hydrogen citrate, and 17% PEG 3350. The optimal reservoir buffer for the PNPase core/RNase E micro-domain-RNA-tungstate crystals is composed of 0.2 M di-ammonium hydrogen citrate, 17% PEG 3350, about pH 4.5, 50 mM disodium tungstate. Crystals for the PNPase core/RNase E micro-domain-Mn2+ co-crystals are prepared using 2.5 M NaCl, 9% (w/v) PEG 6000, 20 mM sodium citrate, and 20 mM manganese acetate tetrahydrate
wild-type and C-terminal KH/S1 domain truncated mutant at resolutions of 2.6 and 2.8 A, respectively. The six PH domains assemble into a ring-like structure containing a central channel
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A552T
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complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance
DELTA549-709
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complementation of growth defect at 15°C of host strain
E371K
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complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance
E81D
-
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity
E81K
-
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity
P98L
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complementation of growth defect at 15°C of host strain, forms of smaller colonies than host strain. Severe reduction of enzyme activity and increased PNPase expression levels
R97C
-
complementation of growth defect at 15°C of host strain. Severe reduction of enzyme activity and increased PNPase expression levels
V304A/V305D
-
complementation of growth defect at 15°C of host strain
V521I
-
complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance
V639D
-
complementation of growth defect at 15°C of host strain, migrates slower than wild-type on SDS-PAGE, forms of smaller colonies than host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity
W233Stop
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complementation of growth defect at 15°C of host strain
A552T
-
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.7, as compared with 1.0 in wild-type
C1310T
-
mutation invovled in sRNA regulation defects
C277T
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mutation invovled in sRNA regulation defects
C943T
-
mutation invovled in sRNA regulation defects
E371K
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ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type
E81D
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impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 1.6, as compared with 1.0 in wild-type
E81K
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impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.4, as compared with 1.0 in wild-type
F635A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
F635A/F638A/H650A
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site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme
F635R/F638R/H650R
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
F638A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
G1307A
-
mutation invovled in sRNA regulation defects
G1466A
-
mutation invovled in sRNA regulation defects
G570C
-
site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme
G570C/V679A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
H650A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
I555T
-
site-directed mutagenesis, the mutant enzyme shows slightly reduced activity compared to the wild-type enzyme
I576A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
I576A/F638A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
I576T
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
I576T/F638A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
I576T/T585A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
K571L
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
K571Q
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
P98L
-
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.03, as compared with 1.0 in wild-type
R100D
-
growth at 37°C, not able to grow at 15°C
R153A/R372A/R405A/R409A
-
site-directed mutagenesis
R319H
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growth at 37°C, not able to grow at 15°C
R398D/R399D
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growth at 37°C, not able to grow at 15°C
R83A
the mutation has little apparent effect on activity but causes the full-length PNPase to stall on RNA oligomers shorter than eight nucleotides
R97C
-
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.1, as compared with 1.0 in wild-type
V304A/V305D
-
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.02, as compared with 1.0 in wild-type
V521I
-
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.5, as compared with 1.0 in wild-type
V639D
-
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
-
10 min, no loss of activity
55
-
unstable above
65
-
rapid and irreversible inactivation
additional information
-
stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to proteolytic digestion
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 3 mg/ml enzyme concentration, 3 years, no loss of activity
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-20°C, dilute solution, at least 2 months, no loss of activity
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Mono-Q column chromatography
ammonium sulfate, DEAE-cellulose, RNA-sepharose
-
recombinant wild-type and mutant enzymes from Escherichia coli strain ENS134-3
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression of enzyme mutant R153A/R372A/R405A/R409A in Escherichia coli strain BL21(DE3)
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expression of wild-type and mutant enzymes in Escherichia coli strain ENS134-3 from modofied plasmid pAW101 and in beta-galactosidase reporter strain IBPC7322(lambdaGF2), overview
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overexpression in Escherichia coli in the presence or absence of increased levels of polyadenylated transcripts
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PNPase regulates its own expression via a reversible RNase III-independent pathway acting upstream from the RNase III-dependent branch. This pathway requires the PNPase RNA binding domains KH and S1 but not its phosphorolytic activity
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after heating at 100°C for 1 min 25-30% of the original activity can be recovered by dissolving the precipitate in 6 M guanidine-HCl followed by dialysis
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refolding of SDS-PAGE purified PNPase diluted 50fold into enzyme buffer containing 0.5% Triton X-100 and 0.5 mg/ml bovine serum albumin
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, Z.; Deutscher, M.P.
An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase
J. Bacteriol.
179
4391-4395
1997
Escherichia coli
Manually annotated by BRENDA team
Littauer, U.Z.; Soreq, H.
Polynucleotide phosphorylase
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
15B
517-553
1982
Achromobacter sp., Achromobacter sp. KR. 170-4, Azotobacter vinelandii, Bacillus amyloliquefaciens, Bacillus amyloliquefaciens BaM-2, Brevibacterium sp., Cavia porcellus, Clostridium perfringens, Enterococcus faecalis, Escherichia coli, Geobacillus stearothermophilus, Halobacterium salinarum, Micrococcus luteus, Nicotiana tabacum, Rattus norvegicus, Rhodospirillum rubrum, Sinorhizobium meliloti, Streptococcus pyogenes, Synechococcus elongatus PCC 7942, Thermus aquaticus
-
Manually annotated by BRENDA team
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
Soreq, H.; Littauer, U.Z.
Purification and characterization of polynucleotide phosphorylase from Escherichia coli. Probe for the analysis of 3 sequences of RNA
J. Biol. Chem.
252
6885-6888
1977
Escherichia coli
Manually annotated by BRENDA team
Smith, J.C.; Eaton, M.A.W.
Purification of polynucleotide phosphorylase by affinity chromatography and some properties of the purified enzymes
Nucleic Acids Res.
1
1763-1773
1974
Escherichia coli, Geobacillus stearothermophilus
Manually annotated by BRENDA team
Carpousis, A.J.; Van Houwe, G.; Ehretsmann, C.; Krisch, H.M.
Copurification of E. coli RNase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation
Cell
76
889-900
1994
Escherichia coli
Manually annotated by BRENDA team
Lisitsky, I.; Schuster, G.
Preferential degradation of polyadenylated and polyuridinylated RNAs by the bacterial exoribonuclease polynucleotide phosphorylase
Eur. J. Biochem.
261
468-474
1999
Escherichia coli
Manually annotated by BRENDA team
Mohanty, B.K.; Kushner, S.R.
Polynucleotide phosphorylase functions both as a 3' -> 5' exonuclease and a poly(A) polymerase in Escherichia coli
Proc. Natl. Acad. Sci. USA
97
11966-11971
2000
Escherichia coli
Manually annotated by BRENDA team
Spickler, C.; Mackie, G.A.
Action of RNase II and polynucleotide phosphorylase against RNAs containing stem-loops of defined structure
J. Bacteriol.
182
2422-2427
2000
Escherichia coli
Manually annotated by BRENDA team
Zangrossi, S.; Briani, F.; Ghisotti, D.; Regonesi, M.E.; Tortora, P.; Deho, G.
Transcriptional and post-transcriptional control of polynucleotide phosphorylase during cold acclimation in Escherichia coli
Mol. Microbiol.
36
1470-1480
2000
Escherichia coli
Manually annotated by BRENDA team
Baginsky, S.; Shteiman-Kotler, A.; Liveanu, V.; Yehudai-Resheff, S.; Bellaoui, M.; Settlage, R.E.; Shabanowitz, J.; Hunt, D.F.; Schuster, G.; Gruissem, W.
Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosome
RNA
7
1464-1475
2001
Escherichia coli, Spinacia oleracea
Manually annotated by BRENDA team
Hayakawa, H.; Kuwano, M.; Sekiguchi, M.
Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein
Biochemistry
40
9977-9982
2001
Escherichia coli
Manually annotated by BRENDA team
Yehudai-Resheff, S.; Hirsh, M.; Schuster, G.
Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
Mol. Cell. Biol.
21
5408-5416
2001
Escherichia coli, Spinacia oleracea
Manually annotated by BRENDA team
Bermudez-Cruz, R.M.; Garcia-Mena, J.; Montanez, C.
Polynucleotide phosphorylase binds to ssRNA with same affinity as to ssDNA
Biochimie
84
321-328
2002
Escherichia coli
Manually annotated by BRENDA team
Mohanty, B.K.; Kushner, S.R.
Polyadenylation of Escherichia coli transcripts plays an integral role in regulating intracellular levels of polynucleotide phosphorylase and RNase E
Mol. Microbiol.
45
1315-1324
2002
Escherichia coli
Manually annotated by BRENDA team
Duran-Figueroa, N.V.; Pina-Escobedo, A.; Schroeder, I.; Simons, R.W.; Garcia-Mena, J.
Polynucleotide phosphorylase interacts with ribonuclease E through a betabetaalphabetabetaalpha domain
Biochimie
88
725-735
2006
Escherichia coli, Escherichia coli (P05055)
Manually annotated by BRENDA team
Briani, F.; Del Favero, M.; Capizzuto, R.; Consonni, C.; Zangrossi, S.; Greco, C.; De Gioia, L.; Tortora, P.; Deho, G.
Genetic analysis of polynucleotide phosphorylase structure and functions
Biochimie
89
145-157
2007
Escherichia coli, Escherichia coli (P05055)
Manually annotated by BRENDA team
Marchi, P.; Longhi, V.; Zangrossi, S.; Gaetani, E.; Briani, F.; Deho, G.
Autogenous regulation of Escherichia coli polynucleotide phosphorylase during cold acclimation by transcription termination and antitermination
Mol. Genet. Genomics
278
75-84
2007
Escherichia coli
Manually annotated by BRENDA team
Amblar, M.; Barbas, A.; Gomez-Puertas, P.; Arraiano, C.M.
The role of the S1 domain in exoribonucleolytic activity: substrate specificity and multimerization
RNA
13
317-327
2007
Escherichia coli, Escherichia coli (P05055)
Manually annotated by BRENDA team
Shi, Z.; Yang, W.Z.; Lin-Chao, S.; Chak, K.F.; Yuan, H.S.
Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation
RNA
14
2361-2371
2008
Escherichia coli, Escherichia coli (P05055)
Manually annotated by BRENDA team
Matus-Ortega, M.E.; Regonesi, M.E.; Pina-Escobedo, A.; Tortora, P.; Deho, G.; Garcia-Mena, J.
The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature
Biochim. Biophys. Acta
1769
194-203
2007
Escherichia coli, Escherichia coli (P05055)
Manually annotated by BRENDA team
Awano, N.; Inouye, M.; Phadtare, S.
RNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase II
J. Bacteriol.
190
5924-5933
2008
Escherichia coli, Escherichia coli JM83
Manually annotated by BRENDA team
Chang, S.A.; Cozad, M.; Mackie, G.A.; Jones, G.H.
Kinetics of polynucleotide phosphorylase: comparison of enzymes from Streptomyces and Escherichia coli and effects of nucleoside diphosphates
J. Bacteriol.
190
98-106
2008
Escherichia coli, Streptomyces coelicolor
Manually annotated by BRENDA team
Carzaniga, T.; Briani, F.; Zangrossi, S.; Merlino, G.; Marchi, P.; Deho, G.
Autogenous regulation of Escherichia coli polynucleotide phosphorylase expression revisited
J. Bacteriol.
191
1738-1748
2009
Escherichia coli, Escherichia coli (P05055)
Manually annotated by BRENDA team
Del Favero, M.; Mazzantini, E.; Briani, F.; Zangrossi, S.; Tortora, P.; Deho, G.
Regulation of Escherichia coli polynucleotide phosphorylase by ATP
J. Biol. Chem.
283
27355-27359
2008
Escherichia coli
Manually annotated by BRENDA team
Nurmohamed, S.; Vaidialingam, B.; Callaghan, A.J.; Luisi, B.F.
Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: Implications for catalytic mechanism and RNA degradosome assembly
J. Mol. Biol.
389
17-33
2009
Escherichia coli (A7ZS61), Escherichia coli
Manually annotated by BRENDA team
Andrade, J.M.; Arraiano, C.M.
PNPase is a key player in the regulation of small RNAs that control the expression of outer membrane proteins
RNA
14
543-551
2008
Escherichia coli, Escherichia coli MG1693
Manually annotated by BRENDA team
Carzaniga, T.; Antoniani, D.; Deho, G.; Briani, F.; Landini, P.
The RNA processing enzyme polynucleotide phosphorylase negatively controls biofilm formation by repressing poly-N-acetylglucosamine (PNAG) production in Escherichia coli C
BMC Microbiol.
12
270
2012
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
Becket, E.; Tse, L.; Yung, M.; Cosico, A.; Miller, J.H.
Polynucleotide phosphorylase plays an important role in the generation of spontaneous mutations in Escherichia coli
J. Bacteriol.
194
5613-5620
2012
Escherichia coli
Manually annotated by BRENDA team
Wong, A.G.; McBurney, K.L.; Thompson, K.J.; Stickney, L.M.; Mackie, G.A.
The S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and autoregulation
J. Bacteriol.
195
2021-2031
2013
Escherichia coli
Manually annotated by BRENDA team
Nurmohamed, S.; Vincent, H.A.; Titman, C.M.; Chandran, V.; Pears, M.R.; Du, D.; Griffin, J.L.; Callaghan, A.J.; Luisi, B.F.
Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli
J. Biol. Chem.
286
14315-14323
2011
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
De Lay, N.; Gottesman, S.
Role of polynucleotide phosphorylase in sRNA function in Escherichia coli
RNA
17
1172-1189
2011
Escherichia coli, Escherichia coli MG1193
Manually annotated by BRENDA team
Carzaniga, T.; Deho, G.; Briani, F.
RNase III-independent autogenous regulation of Escherichia coli polynucleotide phosphorylase via translational repression
J. Bacteriol.
197
1931-1938
2015
Escherichia coli
Manually annotated by BRENDA team
Bandyra, K.J.; Sinha, D.; Syrjanen, J.; Luisi, B.F.; De Lay, N.R.
The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes
RNA
22
360-372
2016
Escherichia coli
Manually annotated by BRENDA team
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