2.7.7.8: polyribonucleotide nucleotidyltransferase
This is an abbreviated version!
For detailed information about polyribonucleotide nucleotidyltransferase, go to the full flat file.
Word Map on EC 2.7.7.8
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2.7.7.8
-
rnase
-
exoribonuclease
-
polya
-
ribonuclease
-
polymerization
-
polyadenylation
-
phosphorolysis
-
degradosome
-
helicase
-
exonuclease
-
exonucleolytic
-
stem-loop
-
luteus
-
micrococcus
-
5'-diphosphate
-
rna-binding
-
kh
-
hfq
-
oligoribonucleotides
-
rna-degrading
-
heteropolymeric
-
antibioticus
-
dead-box
-
lysodeikticus
-
primer-independent
-
synthesis
-
molecular biology
-
medicine
- 2.7.7.8
- rnase
- exoribonuclease
- polya
- ribonuclease
- polymerization
-
polyadenylation
-
phosphorolysis
-
degradosome
- helicase
-
exonuclease
-
exonucleolytic
-
stem-loop
- luteus
- micrococcus
- 5'-diphosphate
-
rna-binding
- kh
- hfq
- oligoribonucleotides
-
rna-degrading
-
heteropolymeric
- antibioticus
-
dead-box
- lysodeikticus
-
primer-independent
- synthesis
- molecular biology
- medicine
Reaction
Synonyms
AtcpPNPase, AtmtPNPase, chloroplast PNPase, cpPNPase, hPNPase(old-35), hPNPaseold-35, nucleoside diphosphate:polynucleotidyl transferase, nucleotidyltransferase, polyribonucleotide, PNP, PNPase, PNPT1, polynucleotide phosphorylase, polyribonucleotide phosphorylase, RNase PH
ECTree
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Substrates Products
Substrates Products on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase
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REACTION DIAGRAM
2',3'-cyclic RNAn + phosphate
RNA(n-1) + a nucleotide diphosphate
-
-
-
?
24-nucleotide RNA molecule + ADP
25-nucleotide RNA molecule + phosphate
-
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
-
-
r
24-nucleotide RNA molecule + phosphate
23-nucleotide RNA molecule + nucleoside diphosphate
-
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
-
-
r
3'-phosphorylated RNA(n) + phosphate
RNA(n-1) + a nucleotide diphosphate
-
enzyme inefficiently degrades 3'-phosphorylated RNA
-
?
microR-221 RNAn+1 + phosphate
microR-221 RNAn + ADP
-
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
-
-
r
microRNAn+1 + phosphate
microRNAn + ADP
-
recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184
-
-
r
pJFD4 HpaI RNA+1 + phosphate
pJFD4 HpaI RNA + nucleoside diphosphate
-
derivative of SP82 phage RNA, arsenate can replace phosphate
-
?
rabbit globin mRNAn+1 + phosphate
ADP + rabbit globin mRNAn
-
only the poly(A) tail of the mRNA is removed
-
?
RNA + ATP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA + CTP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA + GTP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA + UTP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
yeast RNA+1 + phosphate
yeast RNA + nucleoside diphosphate
-
2% of activity with poly(U)
-
?
poly(A) + ADP
poly(A)+1 + phosphate
-
-
no phosphorolysis activity with poly(G)
?
poly(A) + ADP
poly(A)+1 + phosphate
-
-
no phosphorolysis activity with poly(G)
?
poly(A) + ADP
poly(A)+1 + phosphate
-
strong preference for ADP and poly(A) in phosphorolysis and polymerization reaction
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
poly(A) polymerization product containing 8000-13000 nucleotides
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
32% of activity with poly(U) in phosphorolysis reaction
r
poly(A) + ADP
poly(A)+1 + phosphate
-
chloroplast PNPase has both exonuclease and poly(A) polymerase activity, phosphate enhances RNA degradation activity, ADP inhibits degradation and enhances poly(A) polymerization, ADP best substrate
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
primer required for polymerization
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
51% of activity with ADP
21% of activity with poly(U) in phosphorolysis reaction
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
low poly(C) phosphorolysis activity
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
primer required for polymerization
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
much lower activity than with ADP, activity depends on polyribonucleotide primer
-
-
?
poly(G) + GDP
poly(G)+1 + phosphate
-
10% of activity with ADP and poly(A)
less than 15% of phosphorolysis activity with poly(A)
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
primer required for polymerization
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
phosphorolysis at 14% of activity with poly(A)
?
poly(I) + IDP
poly(I)+1 + phosphate
-
48% of activity with ADP
28% of activity with poly(U) in phosphorolysis reaction
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
primer required for polymerization
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
55% of activity with ADP
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
best substrate for phosphorolysis reaction
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
-
lower activity than with poly(A)
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
primer required for polymerization
-
r
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
catalyzes exchange between beta-phosphate of ADP and phosphate, but only in presence of either an oligoribonucleotide bearing an unidentified C-3'-hydroxyl group or of ADP
exchange reaction
-
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
ADP preferred substrate for exchange, little or no reaction occurs with other nucleoside diphosphates
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
ADP, GDP and CDP are better substrates than UDP, IDP and deoxribonucloside diphosphates do not serve as substrate
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
exchange reaction with ADP, CDP, UDP and GDP
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase is involved in tRNA degradation, PNPase is required for efficient 3'-end processing of mRNAs in vivo, but is not sufficient to mediate their degradation, PNPase may function as poly(A) mRNA 3'-5' degrading exonuclease in vivo
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
synthesis of poly(A): no primer addition required if large amounts of enzyme or Mg2+ are used, with small amounts of either component a primer is required, poly(G) synthesis: primer required
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-independent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
arsenolysis of poly(A), poly(C), poly(U) and poly(G)
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
arsenolysis of poly(A), poly(C), poly(U) and poly(G)
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
activity in the absence of a primer, polymerization is stimulated by various polyribonucleotides or RNAs
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
either in the form of a homotrimeric enzyme or associated in a multiprotein complex, the degradosome, PNPase is involved in RNA processing
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase and RNAse II play an essential role in degrading fragments of mRNA generated by prior cleavage by endonucleases
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase accounts for 10% of total mRNA decay, PNPase can bind double stranded DNA, however the affinity is lower than that obtained for both RNA and single stranded DNA binding
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase synthesizes long, highly heteropolymeric poly(A) tails in vivo and accounts for all of the residual polyadenylylation in poly(A) polymerase deficient strains, in addition PNPase is responsible for adding the C and U residues that are found in poly(A) tails in exponentially growing wild-type cultures
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase exonuclease activity plays an essential role in tRNA, mRNA and ribosome metabolism
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase is involved in RNA degradation
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase specifically binds to 8-oxoguanine-containing RNA, it is suggested that PNPase discriminate between oxidized and normal RNA which my contribute to a high fidelity of translation
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
strong preference for ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
catalyzes addition of a single dAMP from dADP onto an oligoribonucleotide, further addition of either dAMP or AMP to (Ap)ndA is very difficult
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer independent enzyme
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
copolymerization of ADP and dADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
synthetic activity enhanced in presence of a primer
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-independent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
purified enzyme is less dependent on a primer than the enzyme in crude extracts
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-independent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
purified enzyme is less dependent on a primer than the enzyme in crude extracts
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ATP-phosphate exchange at one-third the rate observed with ADP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP, GDP and CTP are better substrates than IDP and UDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP best substrate, UDP 55%, CDP 51%, IDP 48% of activity with ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP best substrate, UDP 55%, CDP 51%, IDP 48% of activity with ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
chloroplast PNPase is most probably responsible for polyadenylation of RNA
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-dependent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-dependent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP, GDP, UDP and CDP polymerized to the extent of 7 S size polymer
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-dependent activity
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
required for multiple aspects of the 18S rRNA metabolism
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(I)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
PNPase prefers degradation of polyadenylated and polyuridinylated RNAs due to the high binding affinities for poly(A) and poly(U), no activity with polyguanylated RNA
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
processive phosphorolysis of the poly(A) tail of each globin mRNA chain
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
in addition to its degradative role, PNPase can also function as a polymerase, adding 3' tails to transcripts. The reverse of degradation is favored when nucleoside diphosphate rather than inorganic phosphate is present in excess
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
substrate is synthetic radiolabeled SL9A RNA
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
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
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
in addition to its degradative role, PNPase can also function as a polymerase, adding 3' tails to transcripts. The reverse of degradation is favored when nucleoside diphosphate rather than inorganic phosphate is present in excess
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
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
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(I)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
strong preference for poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
enhanced expression of hPNPase(old-35) via a replication-incompetent adenovirus (Ad.hPNPase(old-35)) in human melanoma cells and normal melanocytes results in a characteristic sensecence-like phenotype. Overexpression of hPNPase(old-35) results in increased production of ROS, leading to activation of the nuclear factor (NF)-kappaB pathway. Ad.hPNPase(old-35) infection promotes degradation of IkappaBalpha and nuclear translocation of NF-kappaB and markedly increased binding of the transcriptional activator p50/p65. Infection with (Ad.hPNPase(old-35)) enhances the production of interleukin-6 and interleukin-8, two classical NF-kappaB-responsive cytokines. hPNPase(old-35) might play a significant role in producing pathological changes associated with aging be generating proinflammatory cytokines via ROS and NF-kappaB
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
poly(A) length of human mitochondrial mRNAs is controlled by polyadenylation by poly(A) polymerase and deadenylation by polynucleotide phosphorylase. Polyadenylation is required for stability of mitochondrial mRNAs
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
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
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
the functional trimeric phosphorylase is capable of digesting single-stranded RNA to produce final products of about 4 nt in length
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(U)
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(U)
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(C)
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of RNA
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
enzyme has no nucleoside diphosphate-polymerization activity
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(U)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
poly(U) best substrate, yeast RNA 2%, poly(A) 32%, poly(I) 28%, poly(C) 21% of the activity with poly(U)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(I)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(C)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
poly(A), poly(U) and poly(C) most effective substrates
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
PNPase enhances the ability of Yersinia pseudotuberculosis to withstand the killing activities of murine macrophages. PNPase is required for the optimal functioning of the Yersinia type three secretion system, an organelle that injects effector proteins directly into host cells. PNPase plays multifaceted roles in enhancing Yersinia survival in response to stressfull conditions
-
-
?
?
-
-
polynucleotide phosphorylase is an exoribonuclease
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is an exoribonuclease
-
-
?
additional information
?
-
-
in the presence of Mn2+ and low-level inorganic phosphate, PNPase degrades single-stranded DNA, the limited end-processing of DNA is regulated by ATP and is inactive in the presence of Mg2+ or high-level inorganic phosphate
-
-
?
additional information
?
-
-
in the presence of Mn2+ and low-level inorganic phosphate, PNPase degrades single-stranded DNA, the limited end-processing of DNA is regulated by ATP and is inactive in the presence of Mg2+ or high-level inorganic phosphate
-
-
?
additional information
?
-
-
suppression of Rho-dependent transcription termination within the enzyme gene and its restoration by enzyme protein is an autogenous regulation circuit that modulates enzyme gene expression during cold acclimation
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is essential for growth at low temperatures, while polymerization activity is not essential. RNase PH domains 1 and 2 of polynucleotide phosphorylase are important for its cold shock function, suggesting that the RNase activity of the enzyme is critical for its essential function at low temperature. Its polymerization activity is dispensable in its cold shock function. The RNase R , which is cold inducible, cannot complement the cold shock function of PNPase
-
-
?
additional information
?
-
-
polyribonucleotide phosphorylase-mediated degradation is a major regulatory event controlling the levels of sRNAs, namely stationary phase regulators MicA and RybB, that are required for the accurate expression of outer membrane proteins. Degradation by PNPase surpasses the effect of endonucleolytic cleavages by RNase E. Polyribonucleotide phosphorylase is an important enzyme in the growth phase adaptation to stationary phase
-
-
?
additional information
?
-
regulates its own expression at the level of mRNA stability and translation
-
-
?
additional information
?
-
-
regulates its own expression at the level of mRNA stability and translation
-
-
?
additional information
?
-
-
examination of phosphorolytic activity. Enzyme is able to digest a substrate with a 3' single-stranded tail as well as a substrate possessing a 3' stem-loop structure. Presence of nucleoside diphosphates has no effect on the phosphorolytic activity
-
-
?
additional information
?
-
under conditions of excess nucleoside diphosphate and low concentrations of phosphate, PNPase catalyses the reverse reaction to add 3' extensions to transcripts
-
-
?
additional information
?
-
-
under conditions of excess nucleoside diphosphate and low concentrations of phosphate, PNPase catalyses the reverse reaction to add 3' extensions to transcripts
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is essential for growth at low temperatures, while polymerization activity is not essential. RNase PH domains 1 and 2 of polynucleotide phosphorylase are important for its cold shock function, suggesting that the RNase activity of the enzyme is critical for its essential function at low temperature. Its polymerization activity is dispensable in its cold shock function. The RNase R , which is cold inducible, cannot complement the cold shock function of PNPase
-
-
?
additional information
?
-
-
PNPase specifically binds a synthetic RNA containing the oxidative lesion 8-hydroxyguanine, PNPase binds to RNA molecules of natural sequence that are oxidatively damaged by treatment with hydrogen peroxide, PNPase binds oxidized RNA with higher affinity than untreated RNA of the same sequence
-
-
?
additional information
?
-
-
PNPase specifically binds a synthetic RNA containing the oxidative lesion 8-hydroxyguanine, PNPase binds to RNA molecules of natural sequence that are oxidatively damaged by treatment with hydrogen peroxide, PNPase binds oxidized RNA with higher affinity than untreated RNA of the same sequence
-
-
?
additional information
?
-
-
polyribonucleotide phosphorylase-mediated degradation is a major regulatory event controlling the levels of sRNAs, namely stationary phase regulators MicA and RybB, that are required for the accurate expression of outer membrane proteins. Degradation by PNPase surpasses the effect of endonucleolytic cleavages by RNase E. Polyribonucleotide phosphorylase is an important enzyme in the growth phase adaptation to stationary phase
-
-
?
additional information
?
-
-
enzyme may play a role in excluding oxidized forms of RNA from the translation mechanism
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is involved in protecting cells and limiting damaged RNA under oxidative conditions
-
-
?
additional information
?
-
-
the apoptosis-inducing activity of polynucleotide phosphorylase is mediated by activation of double-stranded RNAdependent protein kinase. Activation of RNA-dependent protein kinase by polynucleotide phosphorylase precedes phosphorylation of eukaryotic initiation factor-2A and induction of growth arrest and DNA damage-inducible gene 153, GADD153, that culminates in the shutdown of protein synthesis and apoptosis. Activation of RNA-dependent protein kinase by polynucleotide phosphorylase also instigates down-regulation of the antiapoptotic protein Bcl-xL
-
-
?
additional information
?
-
-
no activity with ATP nor the other NTPs, as well as mono phosphate nucleotides. Enzyme degrades polyadenylated and nonpolyadenylated RNA at similar rates
-
-
?
additional information
?
-
-
suppressor of Var1 3 and polynucleotide phosphorylase form a 330-kDa heteropentamer that is capable of efficiently degrading double-stranded RNA substrates in the presence of ATP, the hSUV3-PNPase complex prefers substrates containing a 3' overhang and degrades the RNA in a 3'-to-5' directionality
-
-
?
additional information
?
-
-
PNPase, as a phosphorylase, incorporates phosphate and ADP in degradation and polymerization process, respectively. The specificity of the enzyme for the polymerization reaction is high for ADP, with much less activity for other nucleotide diphosphates and no activity for ATP or other nucleotide triphosphates. The human PNPase displays no preferential activity for polyadenylated RNA like bacterial or chloroplast PNPase
-
-
?
additional information
?
-
full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase
-
-
?
additional information
?
-
-
full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase
-
-
?
additional information
?
-
-
human polynucleotide phosphorylase hPNPaseold-35 is a type I IFN-inducible 3'-5' exoribonuclease, which degrades specific mRNAs and small noncoding RNAs. miR-221, a regulator of the cyclin-dependent kinase inhibitor p27kip1, displays robust downregulation with ensuing up-regulation of p27kip1 by expression of hPNPaseold-35,which also occurs in multiple human melanoma cells upon IFN-beta treatment
-
-
?
additional information
?
-
-
in the cytoplasm, human enzyme, from adenoviral-mediated overexpression, can directly degrade c-myc mRNA by virtue of its 3'-5' exoribonuclease property, and this degradation is specific for c-myc as compared with other mRNAs, such as c-jun, glyceraldehyde 3-phosphate dehydrogenase or GADD 34. In melanoma cells, degradation of microR-221 by hPNPase is more profound compared with other miRNAs
-
-
?
additional information
?
-
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview
-
-
?
additional information
?
-
-
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview
-
-
?
additional information
?
-
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview
-
-
?
additional information
?
-
-
enzyme is involved in tuning the expression of virulence genes and bacterial fitness during infection
-
-
?
additional information
?
-
-
examination of phosphorolytic activity. Enzyme is able to digest a substrate with a 3' single-stranded tail as well as a substrate possessing a 3' stem-loop structure. Presence of nucleoside diphosphates results in decrease of Km value for phosphorolytic activity
-
-
?
additional information
?
-
at the optimal temperature, polynucleotide phosphorylase completely destroys RNAs that possess even a very stable intramolecular secondary structure, but leaves intact RNAs whose 3' end is protected by chemical modification or by hybridization with a complementary oligonucleotide. This allows individual RNAs to be isolated from heterogeneous populations by degrading unprotected species. If oligonucleotide is hybridized to an internal RNA segment, the Tth polynucelotide phosphorylase stalls eight nucleotides downstream of that segment. This allows any arbitrary 5'-terminal fragment of RNA to be prepared with a precision similar to that of run-off transcription, but without the need for a restriction site
-
-
?
additional information
?
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at the optimal temperature, polynucleotide phosphorylase completely destroys RNAs that possess even a very stable intramolecular secondary structure, but leaves intact RNAs whose 3' end is protected by chemical modification or by hybridization with a complementary oligonucleotide. This allows individual RNAs to be isolated from heterogeneous populations by degrading unprotected species. If oligonucleotide is hybridized to an internal RNA segment, the Tth polynucelotide phosphorylase stalls eight nucleotides downstream of that segment. This allows any arbitrary 5'-terminal fragment of RNA to be prepared with a precision similar to that of run-off transcription, but without the need for a restriction site
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additional information
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enzyme affects the expression and activity of the type III secretion system by distinct mechanisms. the RNA-binding subdomain S1-dependent effect on type III secretion system involves an RNA intermediate
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