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
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rnase
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exoribonuclease
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polya
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ribonuclease
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polymerization
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polyadenylation
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phosphorolysis
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degradosome
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helicase
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exonuclease
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exonucleolytic
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stem-loop
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luteus
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micrococcus
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5'-diphosphate
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rna-binding
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kh
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hfq
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oligoribonucleotides
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rna-degrading
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heteropolymeric
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antibioticus
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dead-box
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lysodeikticus
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primer-independent
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synthesis
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molecular biology
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medicine
- 2.7.7.8
- rnase
- exoribonuclease
- polya
- ribonuclease
- polymerization
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polyadenylation
-
phosphorolysis
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degradosome
- helicase
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exonuclease
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exonucleolytic
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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
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2.7.7.8 polyribonucleotide nucleotidyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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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
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r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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either in the form of a homotrimeric enzyme or associated in a multiprotein complex, the degradosome, PNPase is involved in RNA processing
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?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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PNPase and RNAse II play an essential role in degrading fragments of mRNA generated by prior cleavage by endonucleases
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?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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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
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?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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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
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?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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PNPase exonuclease activity plays an essential role in tRNA, mRNA and ribosome metabolism
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-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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PNPase is involved in RNA degradation
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r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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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
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-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
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chloroplast PNPase is most probably responsible for polyadenylation of RNA
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r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
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required for multiple aspects of the 18S rRNA metabolism
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-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
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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
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-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
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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
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-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
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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 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
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-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
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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
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-
?
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
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?
additional information
?
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polynucleotide phosphorylase is an exoribonuclease
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?
additional information
?
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polynucleotide phosphorylase is an exoribonuclease
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?
additional information
?
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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
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-
?
additional information
?
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-
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
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?
additional information
?
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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
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?
additional information
?
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regulates its own expression at the level of mRNA stability and translation
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?
additional information
?
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regulates its own expression at the level of mRNA stability and translation
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-
?
additional information
?
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-
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
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-
?
additional information
?
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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
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?
additional information
?
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enzyme may play a role in excluding oxidized forms of RNA from the translation mechanism
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?
additional information
?
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polynucleotide phosphorylase is involved in protecting cells and limiting damaged RNA under oxidative conditions
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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enzyme is involved in tuning the expression of virulence genes and bacterial fitness during infection
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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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?
