3.1.13.4: poly(A)-specific ribonuclease
This is an abbreviated version!
For detailed information about poly(A)-specific ribonuclease, go to the full flat file.
Word Map on EC 3.1.13.4
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3.1.13.4
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deadenylation
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polya-specific
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rna-binding
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decapping
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polyadenylation
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polya-binding
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nocturnin
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au-rich
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mirna-mediated
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telomere
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trim
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argonaute
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eif4e
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pirnas
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pumilio
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tristetraprolin
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cap-binding
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congenita
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exonucleolytic
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p-bodies
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dyskeratosis
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oligoadenylation
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pabps
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diagnostics
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miriscs
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poly-a
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are-binding
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microrna-mediated
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medicine
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eif4e-binding
- 3.1.13.4
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deadenylation
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polya-specific
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rna-binding
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decapping
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polyadenylation
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polya-binding
- nocturnin
-
au-rich
-
mirna-mediated
-
telomere
-
trim
-
argonaute
- eif4e
-
pirnas
-
pumilio
- tristetraprolin
-
cap-binding
- congenita
-
exonucleolytic
-
p-bodies
-
dyskeratosis
-
oligoadenylation
-
pabps
- diagnostics
-
miriscs
- poly-a
-
are-binding
-
microrna-mediated
- medicine
-
eif4e-binding
Reaction
exonucleolytic cleavage of poly(A) to 5'-AMP =
Synonyms
2',3'-exoribonuclease, 3'-exoribonuclease, adenosine-specific exonuclease, AHG2, AtPARN, BTG1-binding factor 1, Caf1, CCR4, CCR4 deadenylase complex, CCR4-associated factor 1, Ccr4-Not complex, CCR4-NOT transcription complex subunit 7, Ccr4p/Pop2p/Notp complex, CNOT6L nuclease, cytoplasmic deadenylase, deadenylase, hPAN, HsPNLDC1, MMAR_3223, More, nuclease, polyadenylate-specific exoribo-, PAB1P-dependent poly(A)-nuclease, PAN, PAN2, PAN3, PARN, PARN-1, PARN-like domain-containing protein 1, PF2046, PNLDC1, poly(A) nuclease, poly(A) nuclease complex, poly(A) ribonuclease, poly(A)-selective ribonuclease, poly(A)-specific 3'-5' ribonuclease, poly(A)-specific 3'-exoribonuclease, poly(A)-specific mRNA exoribonuclease, poly(A)-specific ribonuclease, poly(A)-specific RNase, Pop2p deadenylase, RNase AS, RNase H
ECTree
3.1.13.4 poly(A)-specific ribonucleaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.1.13.4 - poly(A)-specific ribonuclease
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SUBSTRATE 
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
2',5'-linked oligoadenylates + H2O
5'-AMP
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in interferon treated cells
-
-
?
AAAACAAAAA + H2O
AMP + ?
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plus a further degradation product containing four A nucleotides and one C nucleotide
-
?
polyadenylated RNA containing AU-rich elements + H2O
RNA containing AU-rich elements + AMP
-
-
?
miR-362-5p + H2O
?
miR-362-5p is defined by DROSHA and DICER to 26 nt in length
-
-
?
miR-362-5p + H2O
?
a mammalian miRNA whose precursor contains a relatively large bulge compared with other premiRNAs. Primer extension analysis of miR-362-5p
-
-
?
mRNA-poly(A) + H2O
?
the enzyme is involved in the removal of polyA tails from mRNAs
-
-
?
mRNA-poly(A) + H2O
?
nocturnin removes the poly(A) tail from a synthetic RNA substrate in a process known as deadenylation. It specifically degrades the 3' poly(A) tail
-
-
?
poly(A) RNA + H2O
5'-AMP + ?
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exonucleolytic cleavage of poly(A) in either the single- or double-stranded form (poly(A)*poly(U)) to 5'-AMP (3'-exonucleolytic activity)
-
-
?
poly(A) RNA + H2O
5'-AMP + ?
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does not disintegrate polyribosomes isolated from quail oviduct
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-
?
poly(A) RNA + H2O
5'-AMP + ?
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one RNA-binding domain is required for the substrate binding, but not for the catalysis of PARN
-
-
?
poly(A)-mRNA + H2O
5'-AMP
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PAN mutants have only mild effects on deadenylation
-
-
?
poly(A)-mRNA + H2O
5'-AMP
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PAN RNase does not cut poly(A)tails to lengths below 50 adenylate residues
-
-
?
poly(A)-mRNA + H2O
5'-AMP
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absolute requirement for a ribonucleoprotein
-
-
?
additional information
?
-
-
mRNA deadenylation by exoribonucleolytic activity of PARN is essential for embryogenesis and viability, deadenylation of mRNA is often the first and rate-limiting step in mRNA decay, loss of the enzyme affects poly(A) tail length distribution of only a select subset of embryonic transcripts
-
-
?
additional information
?
-
-
enzyme is 5-6 times more active if the substrate is m7G(5)ppp(5)G capped
-
?
additional information
?
-
-
mRNA deadenylation by exoribonucleolytic activity of PARN is not essential for embryogenesis and viability
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-
?
additional information
?
-
-
enzyme is 5-6 times more active if the substrate is m7G(5)ppp(5)G capped
-
?
additional information
?
-
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physiological role of enzyme, recognition mechanisms that target mRNA for degradation
-
?
additional information
?
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PARN interacts not only with the 3'-end of the mRNA but also with its 5'-end as PARN contains an RNA-recognition motif domain that specifically binds both the poly(A) tail and the 7-methylguanosine cap. The interaction of PARN with the 5'-cap of mRNAs stimulates the deadenylation activity and enhances the processivity of this reaction
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-
?
additional information
?
-
-
PARN specifically degrades the mRNA poly(A) tails with a free 3'-hydroxyl group and releases 5'-AMP as the mononucleotide product
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-
?
additional information
?
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Poly(A)-specific ribonuclease is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails
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-
?
additional information
?
-
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Poly(A)-specific ribonuclease is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails
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-
?
additional information
?
-
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the nuclease domain of CNOT6L exhibits full Mg2+-dependent deadenylase activity with strict poly(A) RNA substrate specificity. The active site of CNOT6L recognizes the RNA substrate through its negatively charged surface
-
-
?
additional information
?
-
active site structure, modelling, overview
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-
?
additional information
?
-
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full-length CNOT6L shows 3'-5' deadenylase activity, the enzyme exhibits a molecular deadenylase mechanism involving a pentacovalent phosphate transition. The 3'-5' deadenylase activity of the CNOT6L catalytic domain alone for poly(A) RNA substrates appears to be increased with 7 nucleotides at the 5' end, or reduced with 25 nucleotides at the 5' end, substrate specificity, overview
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-
?
additional information
?
-
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synthesis of RNA substrates A5 to A20, G20, C20, U20, AAA, GGG, CCC, UUU, AXX, XXA, XAX, AXA, AAX, and XAA, where X denotes G, C, or U, and usage of commercial substrate, a 44-nucleotide heteropolymeric RNA, with sequence 5'-CCA UCU CAU CCC UGC GUG UCC CAU CUG UUC CCU CCC UGU CUC AG-3', substrate specificity of the recombinant enzyme, overview. The active site of PARN per se harbors specificity for recognition of adenosine
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-
?
additional information
?
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enzyme is involved in processing of microRNA. Upon leavage of the 3' arm of the pre-miR-451 precursor hairpin by Argonaute2, the 3' end of the cleaved pre-miR-451 intermediate is then trimmed to the mature length by poly(A)-specific ribonuclease PARN. Trimming requires a 3'-5' exonucleolytic activity, prefers adenosine to uridine and depends on the presence of Mg2+
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-
?
additional information
?
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Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
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-
?
additional information
?
-
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Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
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-
?
additional information
?
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shortening of the poly(A) tail is performed by the multi-subunit Ccr4-Not deadenylase, which contains the Caf1 (Pop2) and Ccr4 catalytic components, and poly(A)-specific ribonuclease (PARN)
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-
?
additional information
?
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shortening of the poly(A) tail is performed by the multi-subunit Ccr4-Not deadenylase, which contains the Caf1 (Pop2) and Ccr4 catalytic components, and poly(A)-specific ribonuclease (PARN)
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-
?
additional information
?
-
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shortening of the poly(A) tail is performed by the multi-subunit Ccr4-Not deadenylase, which contains the Caf1 (Pop2) and Ccr4 catalytic components, and poly(A)-specific ribonuclease (PARN)
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-
?
additional information
?
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enzyme PARN performs exonucleolytic trimming of 18S-E pre-rRNA, and PARN can process the corresponding ITS1 RNA fragment in vitro
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-
?
additional information
?
-
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enzyme PARN performs exonucleolytic trimming of 18S-E pre-rRNA, and PARN can process the corresponding ITS1 RNA fragment in vitro
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-
?
additional information
?
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molecular mechanism of 5' cap recognition by PARN, overview. The PARN cap-binding site is bipartite: Trp475 constitutes the essential binding surface for m7G, while the first transcribed nucleoside is bound by the nuclease domain. The enzyme interacts with m7GpppG, m7Gpppm2'OG, m7GTP, GpppG(macro), GpppG(micro), m2_2.7GTP, and m3_2.2.7GTP. Role of His449 in mRNA 5' cap binding, involvement of His449 in sustaining the proper specificity of the enzyme, overview
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-
?
additional information
?
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usage of synthetic oligoRNA substrates: N9A15, A12, U12, C12, G12 and dA12. Activity modulation experiments in the presence of m7G(5')ppp(5')G cap analogue. The recombinant enzyme exhibits specific deadenylation activity in vitro, with very high specificity for recognition of poly(A) or poly(dA)
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-
?
additional information
?
-
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usage of synthetic oligoRNA substrates: N9A15, A12, U12, C12, G12 and dA12. Activity modulation experiments in the presence of m7G(5')ppp(5')G cap analogue. The recombinant enzyme exhibits specific deadenylation activity in vitro, with very high specificity for recognition of poly(A) or poly(dA)
-
-
?
additional information
?
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PARN is a divalent metal ion-dependent 3'-exonuclease that specifically catalyzes the 3'-5'-degradation of the single-stranded poly(A) tail of mRNA with a free 3'-hydroxyl group
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-
?
additional information
?
-
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PARN is a divalent metal ion-dependent 3'-exonuclease that specifically catalyzes the 3'-5'-degradation of the single-stranded poly(A) tail of mRNA with a free 3'-hydroxyl group
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-
?
additional information
?
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PARN is one of the major mammalian 3'-specific exoribonucleases involved in the degradation of the mRNA poly(A)-tail and it is also involved in the regulation of translation in early embryonic development, it is the key enzyme involved in the deadenylation of mRNA in a cap-dependent manner
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-
?
additional information
?
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PARN is one of the major mammalian 3'-specific exoribonucleases involved in the degradation of the mRNA poly(A)-tail and it is also involved in the regulation of translation in early embryonic development, it is the key enzyme involved in the deadenylation of mRNA in a cap-dependent manner
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-
?
additional information
?
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PARN protein levels are not appreciably altered by lipopolysaccharide stimulation in RAW264.7 macrophage cells
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-
?
additional information
?
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the interaction between PARN and the 7-methylguanosine cap of mRNA plays a key role in stimulating the rate of deadenylation
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-
?
additional information
?
-
-
the interaction between PARN and the 7-methylguanosine cap of mRNA plays a key role in stimulating the rate of deadenylation
-
-
?
additional information
?
-
usage of synthetic oligoRNA substrates: N9A15, A12, U12, C12, G12 and dA12. Activity modulation experiments in the presence of m7G(5')ppp(5')G cap analogue. The recombinant enzyme exhibits specific deadenylation activity in vitro, with very high specificity for recognition of poly(A) or poly(dA)
-
-
?
additional information
?
-
-
usage of synthetic oligoRNA substrates: N9A15, A12, U12, C12, G12 and dA12. Activity modulation experiments in the presence of m7G(5')ppp(5')G cap analogue. The recombinant enzyme exhibits specific deadenylation activity in vitro, with very high specificity for recognition of poly(A) or poly(dA)
-
-
?
additional information
?
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enzyme shows strong specificity toward polyadenylate nucleotides, no degradation of poly(C), poly(G), and poly(U) substrates
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-
?
additional information
?
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RNase H fold protein PF2046 of Pyrococcus furiosus is a 3'-5' ssDNA exonuclease that cleaves after the second nucleotide from the 3' end of ssDNA and prefers poly-dT over poly-dA as a substrate
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-
?
additional information
?
-
RNase H fold protein PF2046 of Pyrococcus furiosus is a 3'-5' ssDNA exonuclease that cleaves after the second nucleotide from the 3' end of ssDNA and prefers poly-dT over poly-dA as a substrate
-
-
?
additional information
?
-
RNase H fold protein PF2046 of Pyrococcus furiosus is a 3'-5' ssDNA exonuclease that cleaves after the second nucleotide from the 3' end of ssDNA and prefers poly-dT over poly-dA as a substrate
-
-
?
additional information
?
-
RNase H fold protein PF2046 of Pyrococcus furiosus is a 3'-5' ssDNA exonuclease that cleaves after the second nucleotide from the 3' end of ssDNA and prefers poly-dT over poly-dA as a substrate
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-
?
additional information
?
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the enzyme plays an important role in the posttranscriptional maturation of mRNA poly(A) tails, factors involved in positive, e.g. Pan3p, and negative, e.g. Pbp1p, regulation, schematic model, overview
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-
?
additional information
?
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-
the poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis and 3' processing to export, Pab1p is essential, but several bypass suppressors exist, deletion leads to exosome-dependent retention at sites of transcription and inefficient nRNA release, e.g. of SSA4 mRNA, Pab1p and PAN interaction mechanism, overview
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-
?
additional information
?
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protein-protein interaction specificity, Pab1p interacts with Pan3p and Pbp1p, which also interact with each other, Pbp1p interacts with itself, binding pocket structures, overview
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-
?
additional information
?
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mRNA deadenylation by exoribonucleolytic activity of PARN is not essential for embryogenesis and viability
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-
?
additional information
?
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isozyme PARN-1 degrades RNA-A60. No activity with RNA-A60 with a 22-heteronucleotide sequence added 3' to the poly(A) tail of RNA-A60 as substrate
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-
?
additional information
?
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isozyme PARN-1 degrades RNA-A60. No activity with RNA-A60 with a 22-heteronucleotide sequence added 3' to the poly(A) tail of RNA-A60 as substrate
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-
?
additional information
?
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enzyme is 5-6 times more active if the substrate is m7G(5)ppp(5)G capped
-
?
