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Information on EC 3.1.13.4 - poly(A)-specific ribonuclease and Organism(s) Homo sapiens and UniProt Accession Q9UIV1
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3.1.13.4 poly(A)-specific ribonucleaseSpecify your search results
Word Map
- 3.1.13.4
-
deadenylation
-
polya-specific
-
rna-binding
-
decapping
-
polyadenylation
-
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
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
deadenylase, ccr4-not complex, parn, poly(a)-specific ribonuclease, rnase as, pnldc1, cytoplasmic deadenylase, poly(a) nuclease, 3'-exoribonuclease, ccr4-associated factor 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2',3'-exoribonuclease
-
-
-
-
3'-exoribonuclease
-
-
-
-
nuclease, polyadenylate-specific exoribo-
-
-
-
-
PAB1P-dependent poly(A)-nuclease
-
-
-
-
PARN
poly(A)-specific 3'-exoribonuclease
-
-
-
-
poly(A)-specific mRNA exoribonuclease
-
-
-
-
poly(A)-specific ribonuclease
additional information
PARN
-
-
PARN
-
additional information
-
the enzyme belongs to the EEP family adopts a complete alpha/beta sandwich fold typical of hydrolases with highly conserved active site residues similar to APE1
additional information
poly(A)-specific ribonuclease belongs to the DEDD superfamily of 3'-exonucleases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
exonucleolytic cleavage of poly(A) to 5'-AMP
mechansim, substrate recognition of mRNA for degradation
-
exonucleolytic cleavage of poly(A) to 5'-AMP
catalytic mechanism for CNOT6L 3'-5' deadenylation involving a pentacovalent phosphate transition, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
110541-21-4
-
215797-47-0
-
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
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
-
-
?
poly(A) RNA + H2O
5'-AMP + ?
-
one RNA-binding domain is required for the substrate binding, but not for the catalysis of PARN
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
-
enzyme is 5-6 times more active if the substrate is m7G(5)ppp(5)G capped
-
?
additional information
?
-
-
physiological role of enzyme, recognition mechanisms that target mRNA for degradation
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
PARN specifically degrades the mRNA poly(A) tails with a free 3'-hydroxyl group and releases 5'-AMP as the mononucleotide product
-
-
?
additional information
?
-
Poly(A)-specific ribonuclease is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails
-
-
?
additional information
?
-
-
Poly(A)-specific ribonuclease is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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+
-
-
?
additional information
?
-
Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
-
-
?
additional information
?
-
-
Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
enzyme PARN performs exonucleolytic trimming of 18S-E pre-rRNA, and PARN can process the corresponding ITS1 RNA fragment in vitro
-
-
?
additional information
?
-
-
enzyme PARN performs exonucleolytic trimming of 18S-E pre-rRNA, and PARN can process the corresponding ITS1 RNA fragment in vitro
-
-
?
additional information
?
-
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
-
-
?
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)
-
-
?
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
miR-362-5p + H2O
?
miR-362-5p is defined by DROSHA and DICER to 26 nt in length
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
-
physiological role of enzyme, recognition mechanisms that target mRNA for degradation
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
PARN specifically degrades the mRNA poly(A) tails with a free 3'-hydroxyl group and releases 5'-AMP as the mononucleotide product
-
-
?
additional information
?
-
Poly(A)-specific ribonuclease is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails
-
-
?
additional information
?
-
-
Poly(A)-specific ribonuclease is a eukaryotic enzyme that efficiently degrades mRNA poly(A) tails
-
-
?
additional information
?
-
-
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
?
-
-
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+
-
-
?
additional information
?
-
Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
-
-
?
additional information
?
-
-
Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
two Mg2+ ions present in the active sites of the ribonucleases of multi-subunit Ccr4-Not deadenylase and are required for RNA cleavage
K+
Mg2+
K+
-
the binding of K+ to the entire RNA-recognition motif domain, which plays a central role in the allosteric communications of PARN regulation, leads to an increase of substrate-binding affinity but a decrease in the cooperativity of the substrate-binding site, while the binding of the cap analogue decreases both the catalytic efficiency and the substrate-binding affinity
K+
K+ is essential to PARN activity and acts as an allosteric activator of PARN with multiple binding sites. K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation
Mg2+
-
can protect PARN against thermal inactivation by increasing the midpoint of inactivation and decreasing the inactivation rate, protective effect is unique to Mg2+ in a concentration-dependent manner
Mg2+
required, the active site of PARN contains four conserved acidic amino acid residues, D28, E30, D292 and D382, the latter being the most important, that coordinate two Mg2+ ions and are essential for the catalytic activity. These acidic residues form a negative charge cave that can bind with two Mg2+ ions. Cofactor Mg2+ is also important to PARN stability against inactivation induced by heat treatment, but promotes thermal aggregation at high temperatures. Mg2+ significantly decreases the rate but increases the aggregate size of the 54 kDa wild-type enzyme in a concentration-dependent manner. The metal cofactor binding or mutation induces changes in the microenvironments around Trp residues
Mg2+
-
the deadenylase activity of CNOT6L is strictly dependent on the presence of Mg2+
Mg2+
two Mg2+ ions present in the active sites of the ribonucleases of multi-subunit Ccr4-Not deadenylase and are required for RNA cleavage
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-hydroxy-3-(3-methylbutyl)-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-3-methyl-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-3-nonyl-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-3-pentyl-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-3-[(morpholin-4-yl)methyl]-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-7-(2-phenylethyl)-3-(3-phenylpropyl)-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-7-[(pyridin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
1-hydroxy-7-[(thiophen-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
3-benzyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
3-decyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
3-dodecyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
3-ethyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
3-hydroxy-6,7,8,9-tetrahydropyrido[2,1-f]purine-2,4(1H,3H)-dione
-
3-[2-(dimethylamino)ethyl]-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
6-hydroxy-1-(2-phenylethyl)-1,4-dihydro-5H-imidazo[4,5-b]pyridin-5-one
-
7-benzyl-1-[(prop-2-en-1-yl)oxy]-3,7-dihydro-1H-purine-2,6-dione
-
NSC-86353
substitution of the benzyl moiety with a methyl group at the N7 position (NSC-85703) reduces the inhibitory activity over 10fold
3-[2-(dimethylamino)ethyl]-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
-
ADP
-
purine monophosphate (RMP) and diphosphate nucleotides (RDP) exhibit competitive inhibition, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
ATP
-
purine triphosphate nucleotides (RTP) behave as non-competitive inhibitors, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
cap analogue 7-methylguanosine(5')ppp(5')G
-
allosteric inhibitor of PARN in the presence of a physiological K+ concentration
deoxyATP
-
purine triphosphate nucleotides (RTP) behave as non-competitive inhibitors, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
deoxyGTP
-
purine triphosphate nucleotides (RTP) behave as non-competitive inhibitors, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
GDP
-
purine monophosphate (RMP) and diphosphate nucleotides (RDP) exhibit competitive inhibition, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
GMP
-
purine monophosphate (RMP) and diphosphate nucleotides (RDP) exhibit competitive inhibition, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
GTP
-
purine triphosphate nucleotides (RTP) behave as non-competitive inhibitors, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
guanidine hydrochloride
-
full-length enzyme retains most of its activity at guanidine hydrochloride concentrations below 0.5 M, whereas an abrupt decrease of the activity of p54 and p46 is found when guanidine hydrochloride concentration is increased
Mg2+
-
behaves as a destabilizer of the overall structural stability of PARN, promotes thermal unfolding and aggregation at high temperatures
purine nucleotides
-
purine triphosphate nucleotides (RTP) behave as non-competitive inhibitors while purine monophosphate (RMP) and diphosphate nucleotides (RDP) exhibit competitive inhibition, furthermore PARN does not discriminate whether there is ribose or deoxy-ribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
-
synthetic fluoro-pyranosyl nucleosides
synthetic nucleoside analogues bearing a fluoroglucopyranosyl sugar moiety and benzoyl-modified cytosine or adenine as a base can effectively inhibit human PARN
-
AMP
-
purine monophosphate (RMP) and diphosphate nucleotides (RDP) exhibit competitive inhibition, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
Poly(A)
strong inhibition of both spermidine- and polyadenylate-binding protein-activated hPAN complex
poly(C)
strong inhibition of spermidine-, slight inhibition of polyadenylate-binding protein-activated hPAN complex
additional information
discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1. Possible interaction modes of 3-hydroxy-pyrimidine-2,4-dione compounds with two divalent metal ions in the active site of Caf1, overview
-
additional information
discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1. Possible interaction modes of 3-hydroxy-pyrimidine-2,4-dione compounds with two divalent metal ions in the active site of Caf1, overview
-
additional information
-
discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1. Possible interaction modes of 3-hydroxy-pyrimidine-2,4-dione compounds with two divalent metal ions in the active site of Caf1, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K+
-
allosteric activator of PARN and its truncated forms, optimal concentration is around 100 mM, with the increase of the K+ concentration, the enzyme reaches its Vmax at a much lower substrate concentration
polyadenylate-binding protein
or spermidine, required for activity of hPAN complex, cannot stimulate hPAN2 alone
-
spermidine
or polyadenylate-binding protein, required for activity of hPAN2 and of hPAN complex
tristetraprolin
required for degradation of polyadenylated RNA containing AU-rich elements
-
additional information
p21 3'-UTR triggers the action of PARN in the AGS cells
-
additional information
-
p21 3'-UTR triggers the action of PARN in the AGS cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
model of cooperative ligand binding by PARN dimer, binding kinetics, dissociation constants, and thermodynamics, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
Poly(A)
residues 1-446 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication
1.1
Poly(A)
residues 1-520 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication
5.6
Poly(A)
N-terminal fragment residues 1-446, pH 7.0, temperature not specified in the publication
7.6
Poly(A)
N-terminal fragment residues 1-520, pH 7.0, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.645
1-(3',4'-dideoxy-3'-fluoro-beta-D-glucopyranosyl) cytosine
at pH 7.0, 30°C
0.21
1-(3',4'-dideoxy-3'-fluoro-beta-D-glucopyranosyl)-N4-benzoyl cytosine
at pH 7.0, 30°C
0.51
9-(3',4'-dideoxy-3'-fluoro-beta-D-glucopyranosyl)-N6-benzoyl adenine
at pH 7.0, 30°C
0.098
poly[2'-O-(2,4-dinitrophenyl)]poly-(A)
pH not specified in the publication, temperature not specified in the publication
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
1-hydroxy-3-(3-methylbutyl)-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0093
1-hydroxy-3-methyl-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0099
1-hydroxy-3-nonyl-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0048
1-hydroxy-3-pentyl-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0087
1-hydroxy-3-[(morpholin-4-yl)methyl]-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0133
1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0021
1-hydroxy-7-(2-phenylethyl)-3-(3-phenylpropyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0106
1-hydroxy-7-(phenoxymethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0106
1-hydroxy-7-(pyridin-2-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0066
1-hydroxy-7-(pyridin-3-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0233
1-hydroxy-7-(pyridin-4-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0104
1-hydroxy-7-phenyl-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.004
1-hydroxy-7-[(pyridin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0036
1-hydroxy-7-[(thiophen-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0145
3-benzyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0207
3-decyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0295
3-dodecyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0122
3-ethyl-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0282
3-hydroxy-6,7,8,9-tetrahydropyrido[2,1-f]purine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.00059
3-[2-(dimethylamino)ethyl]-1-hydroxy-7-(2-phenylethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0151
6-hydroxy-1-(2-phenylethyl)-1,4-dihydro-5H-imidazo[4,5-b]pyridin-5-one
Homo sapiens
pH and temperature not specified in the publication
0.0206
7-(2-butoxyethyl)-1-hydroxy-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0015
7-benzyl-1-hydroxy-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
1
7-benzyl-1-[(prop-2-en-1-yl)oxy]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
1
7-benzyl-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0386
NSC-104148
Homo sapiens
pH and temperature not specified in the publication
0.0287
NSC-116567
Homo sapiens
pH and temperature not specified in the publication
0.525
NSC-193557
Homo sapiens
pH and temperature not specified in the publication
0.251
NSC-85703
Homo sapiens
pH and temperature not specified in the publication
0.0228
NSC-86353
Homo sapiens
pH and temperature not specified in the publication
0.119
1-hydroxy-7-(pyridin-2-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.125
1-hydroxy-7-(pyridin-3-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.245
1-hydroxy-7-(pyridin-4-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0841
1-hydroxy-7-phenyl-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the Kd value of the wild type PARN-RNA-recognition motif enzyme for 7-methylguanosine triphosphate is 6.94 microM
additional information
-
Vmax value is 0.30 micromol/min/micromol for the full-length enzyme at 25 mM K+
additional information
-
Vmax value is 0.36 micromol/min/micromol for the full-length enzyme at 50 mM K+
additional information
-
Vmax value is 0.42 micromol/min/micromol for the full-length enzyme at 100 mM K+
additional information
-
Vmax value is 0.42 micromol/min/micromol for the full-length enzyme at 200 mM K+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
differentiated cells express PNLDC1 only after demethylation
poly(A)-specific ribonuclease (PARN) is upregulated in gastric tumor tissues and gastric cancer cell lines MKN28 and AGS, determination of the expression level of PARN in human gastric cancer cells and tissues by quantitative real-time PCR expression analysis
the expression of deadenylase PARN is differentially expressed in SCC clinical samples. PARN overexpression correlates with younger patient age. Kaplan-Meier analysis suggests that increased levels of PARN correlates with significantly increased survival
the expression of deadenylase PARN is differentially expressed in SCC clinical samples. PARN overexpression correlates with younger patient age. Kaplan-Meier analysis suggests that increased levels of PARN correlates with significantly increased survival
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PNLDC1 is localized predominantly in the endoplasmic reticulum
residues 506-525 in HsPNLDC1-1 represent a putative transmembrane domain
additional information
PARN occurs in the nucleus, upstream of the final endonucleolytic cleavage by the endonuclease NOB1 in the cytoplasm
additional information
PARN, as a component of the pre-40S particle, pulls down with the pre-ribosome factor LTV1 or Bystin. PARN is a constitutive component of the Bystin-associated pre-40S particle
-
additional information
-
PARN, as a component of the pre-40S particle, pulls down with the pre-ribosome factor LTV1 or Bystin. PARN is a constitutive component of the Bystin-associated pre-40S particle
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in eukaryotic cells, cytoplasmic mRNA is characterized by the presence of a 3' poly(A) tail. The median length of the tail varies from 27 to 28 nucleotides in yeast to 60-100 nucleotides in mammalian cells.The tail is important for the control of gene expression, enzymatic shortening of the poly(A) tail (deadenylation) can initiate mRNA degradation and repress translation. An important enzyme involved in cytoplasmic deadenylation is the multi-component Ccr4-Not complex. In addition to six noncatalytic subunits, the complex contains two subunits with ribonuclease activity: both Caf1 and Ccr4 display Mg2+-dependent 3'-'-5' exoribonuclease activity with a preference for poly(A). While the enzymatic activity of Caf1 is associated with an RNAse D/DEDD (Asp-Glu-Asp-Asp) domain, the enzymatic activity of Ccr4 is provided by an EEP (endonuclease-exonuclease-phosphatase) domain
evolution
PARN is a member of the DEDD family of 3'-to-5' exonucleases with a marked nucleotide preference towards A
malfunction
metabolism
physiological function
additional information
malfunction
AGO-APP from parental or PARN knockout cells enrich the miRNAs to a similar extent, without altering the overall length distribution of the miRNA isoforms, suggesting that PARN-mediated trimming does not affect the interaction of miRNAs with AGO proteins
malfunction
depletion of poly(A)-specific ribonuclease (PARN) inhibits proliferation of human gastric cancer cells by blocking cell cycle progression. PARN depletion leads to cell cycle arrest by upregulating p21 expression, stabilizes the p21 mRNA (one of the key regulators in cell growth and survival), and promotes cell death, but does not affect the formation of RNA granules
malfunction
knockdown of PARN or exogenous expression of an enzyme-dead PARN mutant (D28A) accumulates 18S-E in both the cytoplasm and nucleus. Expression of D28A accumulates 18S-E in Bystin-associated pre-40S particles. RNase H-based fragmentation analysis and 3'-sequence analysis of 18S-E species present in cells expressing wild-type PARN or D28A, overview
malfunction
knocking down ribosome biogenesis factors (RBFs) involved in the large subunit pathway (LSG1 and eIF6) has no effect on PARN localization. Co-depletion of PARN and NOB1 yields a much stronger accumulation of 18S-EFL species than the sole knockdown of PARN. This suggests that NOB1 can also cleave untrimmed 18S-E pre-rRNAs, albeit less efficiently. In accordance with this assumption, overexpression of NOB1 in PARN-depleted cells leads to a decreased amount of 18S-EFL pre-rRNA
malfunction
mutations in PARN in patients with haematological and neurological manifestations. Large monoallelic deletions in PARN in four patients with developmental delay or mental illness. One patient in particular has a severe neurological phenotype, central hypomyelination and bone marrow failure. This patient has an additional missense mutation on the non-deleted allele and severely reduced PARN protein and deadenylation activity. Cells from this patient have impaired oligoadenylation of specific H/ACA box small nucleolar RNAs. Importantly, PARN-deficient patient cells manifest short telomeres and an aberrant ribosome profile similar to those described in some variants of dyskeratosis congenita. Knocking down PARN in human marrow cells impaires haematopoiesis. Biallelic mutations in PARN results in severely reduced protein level. PARN-deficient patient cells manifest PARN-associated defects in snoRNA and scaRNA trimming and aberrant ribosome profile. Phenotypes, detailed overview
malfunction
mutations in the PARN gene (encoding poly(A)-specific ribonuclease) cause telomere diseases including familial idiopathic pulmonary fibrosis and dyskeratosis congenita. PARN deficiency impairs telomere maintenance. Mechanism linking PARN mutations to telomere diseases, phenotype analysis, overview
metabolism
3' ends of metazoan microRNAs (miRNAs) are initially defined by the RNase III enzymes during maturation, but subsequently experience extensive modifications by several enzymatic activities. For example, terminal nucleotidyltransferases (TENTs) elongate miRNAs by adding one or a few nucleotides to their 3' ends, which occasionally leads to differential regulation of miRNA stability or function. Poly(A)-specific ribonuclease (PARN) forms the 3' ends of miRNAs in human cells
metabolism
the enzyme plays a role in mRNA catabolism and in exonucleolytic trimming of 18S-E pre-rRNA
metabolism
the expression of several deadenylases is altered in squamous cell lung cancer, SCC. Quantitative real-time PCR shows that four deadenylases, PARN, CNOT6, CNOT7 and NOC, are differentially expressed in SCC clinical samples. PARN overexpression correlates with younger patient age and CNOT6 overexpression with non-metastatic tumors. Kaplan-Meier analysis suggests that increased levels of PARN and NOC correlate with significantly increased survival. The gene expression deregulation is functionally enriched for gene ontologies related to cell adhesion, cell junction, muscle contraction and metabolism
physiological function
poly(A)-specific ribonuclease is involved in the mRNA decay regulation by specifically catalyzing the shortening of the 3'-end poly(A) tail
physiological function
the R3H domain has the ability to bind various oligonucleotides at the micromolar level with no oligo(A) specificity. The removal of the R3H domain dissociates poly(A)-specific ribonuclease into monomers, which still possess the RNA-binding ability and catalytic functions. The removal of the R3H domain does not affect the catalytic pattern of poly(A)-specific ribonuclease. Both R3H domain and RNA-recognition motif domain RRM may be essential for the high affinity of long poly(A) substrate, but the R3H domain does not contribute to the substrate recognition. Compared to the RRM domain, the R3H domain plays a more important role in the structural integrity of the dimeric poly(A)-specific ribonuclease
physiological function
deadenylation regulates RNA function and fate. Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA
physiological function
PNLDC1 is a deadenylase that is excluded from the nucleus and most likely, its function occurs mainly in the endoplasmic reticulum
physiological function
poly(A)-specific ribonuclease (PARN) catalyzes the degradation of mRNA poly(A) tail to regulate translation efficiency and mRNA decay in higher eukaryotic cells. PARN has the unique properties of 5'-cap-binding ability, high activity, allosteric regulation, processive catalysis and highly regulated deadenylation in the cells
physiological function
poly(A)-specific ribonuclease (PARN) forms the 3' ends of miRNAs in human cells. PARN digests the 3' extensions of miRNAs that are derived from the genome or attached by TENTs, thereby effectively reducing the length of miRNAs. PARN-mediated shortening has little impact on miRNA stability, suggesting that this process likely operates to finalize miRNA maturation, rather than to initiate miRNA decay. PARN-mediated shortening is pervasive across most miRNAs and appears to be a conserved mechanism contributing to the 3' end formation of vertebrate miRNAs. PARN has the unique ability to interact with the 7-methylguanosine cap of mRNAs. Enzyme PARN functions as a trimmer to digest the genome-encoded 3' extensions of miRNAs, and PARN shapes the 3' ends of microRNAs as a de-tailor to erase or reduce the size of untemplated nucleotide additions. PARN emerges as a miR-362-5p trimmer in vitro and in vivo, and as general miRNA trimmer
physiological function
poly(A)-specific ribonuclease (PARN) mediates 3'-end maturation of the telomerase RNA component. PARN is required for removal of post-transcriptionally acquired oligo(A) tails that target nuclear RNAs for degradation. Diminished TERC levels and the increased proportion of oligo(A) forms of TERC are normalized by restoring PARN, which is limiting for TERC maturation in cells. Role for PARN in the biogenesis of TERC. TERC serves as the RNA template and scaffold for the telomerxadase reverse-transcriptase holoenzyme
physiological function
poly(A)-specific ribonuclease is a nuclear ribosome biogenesis factor involved in human 18S rRNA maturation. The enzyme supports the processing of different types of non-coding RNAs including telomerase RNA. PARN is part of the enzymatic machinery that matures the human 18S ribosomal RNA (rRNA). PARN is required for 40S ribosomal subunit production. Function of PARN in exonucleolytic trimming of 18S-E pre-rRNA. A number of nucleolar 40S-specific ribosome biogenesis factors (RBFs), including ENP1, DIM2, RRP12, LTV1 and TSR1, accompany pre-40S particles from the nucleolus via the nucleoplasm to the cytosol. Like shuttling nucleolar RBFs, PARN redistributes from the nucleolus to the nucleoplasm upon inhibition of pre-40S particle export by leptomycin B. PARN is coupled to a poly(A) polymerase for processing of the 18S-E pre-rRNA. PARN is primarily involved in pre-rRNA processing, not in quality control
physiological function
poly(A)-specific ribonuclease regulates the processing of small-subunit rRNAs in human cells, poly(A)-specific ribonuclease (PARN) participates in steps leading to 18S-E maturation in human cells. Ribosome biogenesis occurs successively in the nucleolus, nucleoplasm, and cytoplasm. Maturation of the ribosomal small subunit is completed in the cytoplasm by incorporation of a particular class of ribosomal proteins and final cleavage of 18S-E pre-rRNA (18S-E). The enzymatic activity of PARN is necessary for the release of 18S-E from Bystin-associated pre-40S particles. PARN degrades the extended regions encompassing nucleotides 5-44 at the 3' end of mature 18S rRNA
physiological function
the action of PARN strongly relies on protein expression profiles of the cells, which leads to heterogeneity in the stability of PARN-targeted mRNAs
physiological function
PARN, nocturnin and Angel are three of the multiple deadenylases that have been described in eukaryotic cells. While each of these enzymes appears to target poly(A) tails for shortening and influence RNA gene expression levels and quality control, the enzymes differ in terms of enzymatic mechanisms, regulation and biological impact. PARN plays a role in early development, DNA damage and possibly cancer
additional information
alterations in the active site structure by metal binding or mutations might lead to a global conformational change of the enzyme PARN molecule
additional information
-
the active site of PARN per se harbors specificity for recognition of adenosine
additional information
isozyme PARN contains a characteristic nuclear localisation signal (NLS, residues 520-540), a carboxy terminal domain (CTD, 540-639) which are not conserved in PNLDC1 and additional regions, which are absent in PNLDC1. The RRM domain of PARN (445-520) is partially conserved in PNLDC1. HsPNLDC1 active site model, overview. RNA-binding sites of HsPNLDC1, comparison to HsPARN revealing similarities in the spatial arrangement of the catalytic DEDDh-motif and other RNA-interacting residues
additional information
-
isozyme PARN contains a characteristic nuclear localisation signal (NLS, residues 520-540), a carboxy terminal domain (CTD, 540-639) which are not conserved in PNLDC1 and additional regions, which are absent in PNLDC1. The RRM domain of PARN (445-520) is partially conserved in PNLDC1. HsPNLDC1 active site model, overview. RNA-binding sites of HsPNLDC1, comparison to HsPARN revealing similarities in the spatial arrangement of the catalytic DEDDh-motif and other RNA-interacting residues
additional information
poly(A)-specific ribonuclease (PARN) is a dimeric exoribonuclease that efficiently degrades mRNA 3' poly(A) tails while also simultaneously interacting with the mRNA 5' cap. The mRNA 5' cap structure plays a pivotal role in coordination of eukaryotic translation and mRNA degradation. Molecular recognition of mRNA 5' cap by 3' poly(A)-specific ribonuclease (PARN) differs from interactions known for other cap-binding proteins: 1. the auxiliary biological function of 5' cap binding by the 3' degrading enzyme is accomplished by negative cooperativity of PARN dimer subunits, 2. non-coulombic interactions are major factors in the complex formation, and 3. PARN has versatile activity toward alternative forms of the cap. These characteristics contribute to stabilization of the PARN-cap complex needed for the deadenylation processivity. Fluorescence and NMR spectroscopic analysis. Model of cooperative ligand binding by PARN dimer. Enzyme-ligand (cap and cap analogues) interaction analysis by surface plasmon resonance, local conformational changes of PARN upon 5' mRNA cap binding, small increase in the beta-strand and coil contributions and complex formation in the vicinity of the residues Trp475 and Asp478. PARN seems to recognize the 5' cap in a simple fashion by virtue of the single-sided stacking that is unique among cap-binding proteins
additional information
the C-terminal domain (CTD) prevents PARN from thermal inactivation but promotes thermal aggregation to initiate at a temperature much lower than that required for inactivation and unfolding
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CNOT7_HUMAN
285
0
32745
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
135007
x * 135007, catalytic subunit hPAN2, + x * 75886, regulatory subunit hPAN3, calculated from amino acid sequence
54000
74000
75886
x * 135007, catalytic subunit hPAN2, + x * 75886, regulatory subunit hPAN3, calculated from amino acid sequence
74000
4 * 74000, calculated. Poly(A)-specific ribonuclease PARN can self-associate into tetramer and high-order oligomers both in vitro and in living cells. PARN oligomerization is triggered by the R3H domain,which leads to the solvent-exposed Trp219 fluorophore to become buried in a solvent-inaccessible microenvironment. The RRM and C-terminal domains are involved in modulating the dissociation rate of the tetrameric PARN. Tetramerization does not affect the catalytic behavior of the full-length PARN and truncated enzymes containing the RRM domain. Tetramerization significantly enhances the catalytic activity and processivity of the truncated form with the removal of the RRM and C-terminal domains
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
gel filtration experiments show that the PARN-RNA-recognition motif domain predominantly exists as a monomer, but about 5% elute at a volume corresponding to a homodimer
tetramer
4 * 74000, calculated. Poly(A)-specific ribonuclease PARN can self-associate into tetramer and high-order oligomers both in vitro and in living cells. PARN oligomerization is triggered by the R3H domain,which leads to the solvent-exposed Trp219 fluorophore to become buried in a solvent-inaccessible microenvironment. The RRM and C-terminal domains are involved in modulating the dissociation rate of the tetrameric PARN. Tetramerization does not affect the catalytic behavior of the full-length PARN and truncated enzymes containing the RRM domain. Tetramerization significantly enhances the catalytic activity and processivity of the truncated form with the removal of the RRM and C-terminal domains
additional information
?
x * 135007, catalytic subunit hPAN2, + x * 75886, regulatory subunit hPAN3, calculated from amino acid sequence
?
x * 61300, isozyme 1 of HsPNLDC1, sequence calculation, x * 60100, isozyme 2 of HsPNLDC1, sequence calculation
homodimer
gel filtration experiments show that the PARN-RNA-recognition motif domain predominantly exists as a monomer, but about 5% elute at a volume corresponding to a homodimer
homodimer
PARN mainly exists as a homodimer in solutions, while it can also associate into larger oligomers via its R3H domain
additional information
the full length PARN enzyme contains three well-defined domains: the catalytic domain, the R3H domain, and the RNA-recognition motif, RRM
additional information
the human enzyme is composed of at least three functional domains, i.e. the catalytic nuclease domain and two RNA binding domains, the R3H and the RNA recognition motif, respectively, detailed analysis of the global architecture of the human enzyme and dimensions of the full-length protein at subnanometer resolution, by atomic force microscopy imaging, overview
additional information
-
the human enzyme is composed of at least three functional domains, i.e. the catalytic nuclease domain and two RNA binding domains, the R3H and the RNA recognition motif, respectively, detailed analysis of the global architecture of the human enzyme and dimensions of the full-length protein at subnanometer resolution, by atomic force microscopy imaging, overview
additional information
full-length PARN is a multi-domain protein containing the catalytic nuclease domain, the R3H domain, the RRM domain and the C-terminal intrinsically unstructured domain (CTD). Impact of CTD on PARN stability and aggregatory potency, comparing the thermal inactivation and denaturation behaviors of full-length PARN with two N-terminal fragments lacking CTD. K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation. The CTD prevents PARN from thermal inactivation but promotes thermal aggregation to initiate at a temperature much lower than that required for inactivation and unfolding. Domain architecture of PARN and effects of K+ on p74, p60 and p46 secondary and tertiary structures, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
in leukemic cells from patients with acute lymphoblastic leukemia, a significant amount of poly(A)-specific ribonuclease is phosphorylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the PARN-RNA-recognition motif domain (residues 445-540) with a bound 7-methylguanosine triphosphate nucleotide shows a remarkable conformational flexibility of the RNA-recognition motif domain, crystal structure is refined at a resolution of 2.1 A, protein folds into a three-stranded antiparallel beta-sheet that is flanked by one alpha-helix connecting beta-strands beta1 and beta2
in silico model for catalytic mechanism and development of a 3D pharmacophore model. Residues Arg99 and Gln109 are involved in the regulation of catalysis. The natural preference of the enzyme for poly(A) is based on favorable biophysical electrostatic and hydrophobic interactions
purified recombinant CNOT6L nuclease domain in complex with AMP and poly(A) DNA, hanging drop vapour diffusion method, 0.001 ml of protein solution, containing 15 mg/ml protein and 1 mM DTT, is mixed with 0.001 ml of reservoir solution and equilibrated over 300 ml reservoir solution, containing 0.1 M HEPES, pH 7.5, 1.1 M ammonium tartrate, and 0.2 M NDSB-201, at 16°C, X-ray diffraction structure determination and analysis at 1.94-2.44 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D28A
D292A
D382A
D478A
generated by site-directed mutagenesis, Kd value for 7-methylguanosine triphosphate is 20.0 microM
E30A
F484A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
H449A
site-directed mutagenesis, the mutant shows loss of the negative cooperativity between the PARN dimer subunits that is evident for the m7GpppG and m7GTP binding by the wild-type protein
K454A
generated by site-directed mutagenesis, Kd value for 7-methylguanosine triphosphate is 20.03 microM
L197A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
L216A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
L291A
-
site-directed mutagenesis, activity and kinetics with RNA substrates compared to the wild-type enzyme
L414A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
M425A
-
site-directed mutagenesis, activity and kinetics with RNA substrates compared to the wild-type enzyme
N412A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
P365A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
P365A/F484A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
P365A/N412A/F484A
-
site-directed mutagenesis, active site mutant, not expressable in Escherichia coli
T458A
generated by site-directed mutagenesis, Kd value for 7-methylguanosine triphosphate is 30.58 microM
additional information
D28A
site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows unaltered ellipticity
D28A
site-directed mutagenesis, catalytically inactive mutant, phenotype, overview
D292A
site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows unaltered ellipticity
D382A
site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows slightly decreased ellipticity
E30A
site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows significantly decreased ellipticity
additional information
-
PARN(443-560/W456/W475A) mutant is severely defective in cap binding, has RNA binding properties
additional information
-
removal of the R3H domain (mutant p74DR3H) leads to a dramatic decrease in the thermal stability of PARN, while removal of the RRM domain or both of the two RNA-binding domains only results in a minor decrease in PARN stability against thermal inactivation and denaturation
additional information
construction of deletion mutants, i.e. expression of the N-terminal fragment residues 1-540, the N-terminal fragment residues 1-520, the N-terminal fragment residues 1-470, the N-terminal fragment residues 1-446, residues 1-520 with the deletion of the R3H domain, residues 1-446 with the deletion of the R3H domain. N-terminal fragment residues 1-446, residues 1-520 with the deletion of the R3H domain, residues 1-446 with the deletion of the R3H domain display 30.9%, 5.9% and 2.5% of the catalytic efficiency of the N-terminal fragment residues 1-520, respectively
additional information
generation of PARN knockout cells by CRISPR/Cas9-mediated gene knockout. Complementation of PARN activity restores the normal isoform ratio of miR-362-5p in HEK-293T cells
additional information
stable knockdown of the endogenous PARN in the gastric cancer MKN28 and AGS cells. PARN depletion significantly inhibits the proliferation of the two types of gastric cancer cells and promotes cell death, but does not significantly affect cell motility and invasion. The depletion of PARN arrests the gastric cancer cells at the G0/G1 phase by upregulating the expression levels of p53 and p21 but not p27. The mRNA stability of p53 is unaffected by PARN-knockdown in both types of cells. A significant stabilizing effect of PARN-depletion on p21 mRNA is observed in the AGS cells but not in the MKN28 cells
additional information
-
stable knockdown of the endogenous PARN in the gastric cancer MKN28 and AGS cells. PARN depletion significantly inhibits the proliferation of the two types of gastric cancer cells and promotes cell death, but does not significantly affect cell motility and invasion. The depletion of PARN arrests the gastric cancer cells at the G0/G1 phase by upregulating the expression levels of p53 and p21 but not p27. The mRNA stability of p53 is unaffected by PARN-knockdown in both types of cells. A significant stabilizing effect of PARN-depletion on p21 mRNA is observed in the AGS cells but not in the MKN28 cells
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 55
thermal stability and aggregation kinetic parameters, the aggregation is dominated by a first-order kinetics, increase in t0 and the decrease in k implies that Mg2+ can inhibit the rate of enzyme aggregation, overview. Cofactor Mg2+ is also important to PARN stability against inactivation induced by heat treatment, but promotes thermal aggregation at high temperatures. Mg2+ significantly decreases the rate but increases the aggregate size of the 54 kDa wild-type enzyme in a concentration-dependent manner. Effect of mutations on the Mg2+-dependent enzyme thermal aggregation, overview
49
55 - 85
thermal denaturation of PARN in presence or absence of K+, overview
49
-
in the absence of Mg2+, the activity of PARN decreases continuously with increasing temperature
49
-
inactivation of the four PARNs at 49°C, p74 is more stable than p54, p54 is equally stable than mutant p54DR3H, mutant p54DR3H is more stable than mutant p74DR3H
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cell lysis is performed in a buffer containing 400 mM NaCl, 50 mM Tris/HCl, pH 8.0, 2 mM ethylenediaminetetraacetic acid and 2 mM dithiothreitol. The supernatant of the lysate is loaded onto a glutathione-Sepharose column and is eluted with lysis buffer containing 30 mM reduced glutathione. Glutathione S-transferase-PARN-RNA-recognition motif is incubated with protease and a final gel filtration is performed using a buffer containing 300 mM NaCl, 20 mM Tris/HCl, pH 8.0, and 2 mM DTT. PARN-RNA-recognition motif is concentrated to 8.8 mg/ml using a vivaspin concentrator, and 7-methylguanosine triphosphate is added in 6fold molar excess. SeMet-containing PARN-RNA-recognition motif purification is analogous, with the exception that the DTT concentration is elevated to 5 mM.
His-tag affinity chromatography HiTrap Q HP and 7-Me-GTP-Sepharose affinity chromatography
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PARNn purified by glutathione-Sepharose 4B, MonoQ and Superdex 200 gel filtration columns. truncated PARN including the putative cap-binding domain purified by TALON affinity resin. full length PARN purified by Ni-NTA column
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged full-length enzyme and His-tagged enzyme fragment from Escherichia coli strain BL21(DE3)
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta by nickel affinity tandem chromatography and anion exchange chromatography
recombinant wild-type and mutant E240A, D489A, and H529A CNOT6L nuclease domains from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA fragment corresponding to amino acids 443-560 in the human PARN sequence cloned into pCR 2.1TOPO vector and subsequently subcloned into the pET19b vector, recombinant PARN or PARN mutants expressed in Escherichia coli strain BL21(DE3)
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expressed as N-terminal His6-tagged polypeptide in Escherichia coli BL21(DE3)
expression of wild-type and mutants of the truncated catalytic domain of human CNOT6L, residues 158-555, in Escherichia coli
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gene PARN, DNA and amino acid sequence determination and analysis, genotyping, quantitative real-time PCR enzyme expression analysis
gene PARN, expression of His-tagged enzyme in Escherichia coli strain Bl21(DE3)
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gene PARN, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PARN, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta
gene PNLDC1, human PNLDC1-1 and PNLDC1-2 exons arrangement, recombinant expression of EGFP-tagged enzyme in HEK-293 cells, enzyme HsPNLDC1 is produced in two isoforms by alternative splicing of the full-length transcript that contains 19 exons, the peptide residues 1-25 (MDVGADEFEESLPLLQELVQEADFV) of isoform 1 are replaced by the peptide residues 1-14 (MFCTRGLLFFAFLA) in isoform 2 (according to the NCBI annotation), recombinant expression of His-tagged enzyme in Escherichia coli
His-tagged full-length enzyme, comprising residues 1-639, and His-tagged enzyme fragment, PARN(443-560), containing the RNA recognition motif with a 50 amino acids long C-terminal tail, comprising residues 443-560, are expressed in Escherichia coli strain BL21(DE3)
plasmid pET33 containing the human parn gene expressed in Escherichia coli BL21(DE3)
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The PARN fragment comprising amino acids 445-540 is amplified from a human cDNA library and cloned into the expression vector, the glutathione S-transferase-PARN-RNA-recognition motif fusion protein is expressed in Escherichia coli BL21(DE3). PARN mutants are generated from the wild-type clone (pGEX-6P-1 PARN445-540) using a Site-Directed Mutagenesis Kit. SeMet-containing PARN-RNA-recognition motif is expressed in Escherichia coli.
expressed as N-terminal His6-tagged polypeptide in Escherichia coli BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of several deadenylases is altered in squamous cell lung cancer, SCC. Quantitative real-time PCR shows that four deadenylases, PARN, CNOT6, CNOT7 and NOC, are differentially expressed in SCC clinical samples. PARN overexpression correlates with younger patient age and CNOT6 overexpression with non-metastatic tumors. Kaplan-Meier analysis suggests that increased levels of PARN and NOC correlate with significantly increased survival. The gene expression deregulation is functionally enriched for gene ontologies related to cell adhesion, cell junction, muscle contraction and metabolism
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
clinical significance of deadenylases PARN and NOC on the survival in SCC diagnosed patients
medicine
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leukemic cells from patients with acute lymphoblastic leukemia and acute myeloid leukemia display altered expression for CNOT6, CNOT6L, CNOT7 deadenylase and poly(A)-specific ribonuclease with most significant alterations for poly(A)-specific ribonuclease and CNOT7 mRNA levels. In acute lymphoblastic leukemia, a significant amount of poly(A)-specific ribonuclease is phosphorylated
additional information
additional information
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Mg2+ has dual effects on PARN stability, protecting the active site against denaturation, but destabilizing the overall structural stability of the protein
additional information
-
R3H domain may stabilize PARN by acting as a protector or intermolecular chaperone of the RRM domain
additional information
-
RRM motif of PARN harbors both poly(A) and cap binding properties, RRM plays an important role in PARN activity, i.e. recognition and dependence on both the cap structure and poly(A) tail during poly(A) hydrolysis. Trp475 plays an essential role in PARN cap recognition, whereas Glu455 and especially Trp456 play auxiliary roles. Cap binding is not essential for the hydrolytic activity of PARN. Cap and RNA-binding sites of the RRM are structurally and functionally separated from each other
additional information
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the entire RRM domain not only contributes to the substrate binding and efficient catalysis of PARN, but also stabilizes the overall structures of the protein. p46 contains only one Trp residue (W219), p54 contains two (W219 and W456), and p74 contains six (W219, W456, W474, W526, W531 and W639)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Korner, C.G.; Wormington, M.; Muckenthaler, M.; Schneider, S.; Dehlin, E.; Wahle, E.
The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes
EMBO J.
17
5427-5437
1998
Bos taurus, Xenopus sp., Homo sapiens (O95453), Homo sapiens
Ren, Y.G.; Martinez, J.; Virtanen, A.
Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage
J. Biol. Chem.
277
5982-5987
2002
Homo sapiens
Uchida, N.; Hoshino, S.i.; Katada, T.
Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein
J. Biol. Chem.
279
1383-1391
2004
Homo sapiens (Q504Q3), Homo sapiens
Virtanen, A.; Martinez, J.; Ren, Y.G.
Purification of poly(A)-specific ribonuclease
Methods Enzymol.
342
303-309
2001
Bos taurus, Homo sapiens, Xenopus sp.
Gao, M.; Fritz, D.T.; Ford, L.P.; Wilusz, J.
Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro
Mol. Cell
5
479-488
2000
Homo sapiens
Lai, W.S.; Kennington, E.A.; Blackshear, P.J.
Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease
Mol. Cell. Biol.
23
3798-3812
2003
Homo sapiens (O95453)
Wu, M.; Reuter, M.; Lilie, H.; Liu, Y.; Wahle, E.; Song, H.
Structural insight into poly(A) binding and catalytic mechanism of human PARN
EMBO J.
24
4082-4093
2005
Homo sapiens (O95453), Homo sapiens
Nilsson, P.; Virtanen, A.
Expression and purification of recombinant poly(A)-specific ribonuclease (PARN)
Int. J. Biol. Macromol.
39
1-3
2006
Homo sapiens
Seal, R.; Temperley, R.; Wilusz, J.; Lightowlers, R.N.; Chrzanowska-Lightowlers, Z.M.
Serum-deprivation stimulates cap-binding by PARN at the expense of eIF4E, consistent with the observed decrease in mRNA stability
Nucleic Acids Res.
33
376-387
2005
Homo sapiens
Zhang, A.; Liu, W.F.; Yan, Y.B.
Role of the RRM domain in the activity, structure and stability of poly(A)-specific ribonuclease
Arch. Biochem. Biophys.
461
255-262
2007
Homo sapiens
Liu, W.; Zhang, A.; He, G.; Yan, Y.
The R3H domain stabilizes poly(A)-specific ribonuclease by stabilizing the RRM domain
Biochem. Biophys. Res. Commun.
360
846-851
2007
Homo sapiens
Liu, W.F.; Zhang, A.; Cheng, Y.; Zhou, H.M.; Yan, Y.B.
Effect of magnesium ions on the thermal stability of human poly(A)-specific ribonuclease
FEBS Lett.
581
1047-1052
2007
Homo sapiens
Nilsson, P.; Henriksson, N.; Niedzwiecka, A.; Balatsos, N.A.; Kokkoris, K.; Eriksson, J.; Virtanen, A.
A multifunctional RNA recognition motif in poly(A)-specific ribonuclease with cap and poly(A) binding properties
J. Biol. Chem.
282
32902-32911
2007
Homo sapiens
Liu, W.F.; Zhang, A.; Cheng, Y.; Zhou, H.M.; Yan, Y.B.
Allosteric regulation of human poly(A)-specific ribonuclease by cap and potassium ions
Biochem. Biophys. Res. Commun.
379
341-345
2009
Homo sapiens
Monecke, T.; Schell, S.; Dickmanns, A.; Ficner, R.
Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m(7)G-cap-binding mode
J. Mol. Biol.
382
827-834
2008
Homo sapiens (O95453)
Balatsos, N.A.; Vlachakis, D.; Maragozidis, P.; Manta, S.; Anastasakis, D.; Kyritsis, A.; Vlassi, M.; Komiotis, D.; Stathopoulos, C.
Competitive inhibition of human poly(A)-specific ribonuclease (PARN) by synthetic fluoro-pyranosyl nucleosides
Biochemistry
48
6044-6051
2009
Homo sapiens (O95453), Homo sapiens
Balatsos, N.A.; Anastasakis, D.; Stathopoulos, C.
Inhibition of human poly(A)-specific ribonuclease (PARN) by purine nucleotides: kinetic analysis
J. Enzyme Inhib. Med. Chem.
24
516-523
2009
Homo sapiens
Niedzwiecka, A.; Lekka, M.; Nilsson, P.; Virtanen, A.
Global architecture of human poly(A)-specific ribonuclease by atomic force microscopy in liquid and dynamic light scattering
Biophys. Chem.
158
141-149
2011
Homo sapiens (Q96LI5), Homo sapiens
Wang, H.; Morita, M.; Yang, X.; Suzuki, T.; Yang, W.; Wang, J.; Ito, K.; Wang, Q.; Zhao, C.; Bartlam, M.; Yamamoto, T.; Rao, Z.
Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity
EMBO J.
29
2566-2576
2010
Homo sapiens
He, G.J.; Liu, W.F.; Yan, Y.B.
Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(a)-specific ribonuclease
Int. J. Mol. Sci.
12
2901-2916
2011
Homo sapiens (O95453)
Henriksson, N.; Nilsson, P.; Wu, M.; Song, H.; Virtanen, A.
Recognition of adenosine residues by the active site of poly(A)-specific ribonuclease
J. Biol. Chem.
285
163-170
2010
Homo sapiens
Maragozidis, P.; Karangeli, M.; Labrou, M.; Dimoulou, G.; Papaspyrou, K.; Salataj, E.; Pournaras, S.; Matsouka, P.; Gourgoulianis, K.I.; Balatsos, N.A.
Alterations of deadenylase expression in acute leukemias: evidence for poly(A)-specific ribonuclease as a potential biomarker
Acta Haematol.
128
39-46
2012
Homo sapiens
He, G.J.; Zhang, A.; Liu, W.F.; Yan, Y.B.
Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis
Biochim. Biophys. Acta
1834
1089-1098
2013
Homo sapiens (O95453)
He, G.J.; Yan, Y.B.
Self-association of poly(A)-specific ribonuclease (PARN) triggered by the R3H domain
Biochim. Biophys. Acta
1844
2077-2085
2014
Homo sapiens (O95453)
Yoda, M.; Cifuentes, D.; Izumi, N.; Sakaguchi, Y.; Suzuki, T.; Giraldez, A.J.; Tomari, Y.
Poly(A)-specific ribonuclease mediates 3-end trimming of Argonaute2-cleaved precursor microRNAs
Cell Rep.
5
715-726
2013
Homo sapiens
Vlachakis, D.; Pavlopoulou, A.; Tsiliki, G.; Komiotis, D.; Stathopoulos, C.; Balatsos, N.; Kossida, S.
An integrated in silico approach to design specific inhibitors targeting human poly(A)-specific ribonuclease
PLoS ONE
7
e51113
2012
Homo sapiens (O95453), Homo sapiens
He, G.; Yan, Y.
Contributions of the C-terminal domain to poly(A)-specific ribonuclease (PARN) stability and self-association
Biochem. Biophys. Rep.
18
100626
2019
Homo sapiens (O95453)
-
Zhang, L.; Yan, Y.
Depletion of poly(A)-specific ribonuclease (PARN) inhibits proliferation of human gastric cancer cells by blocking cell cycle progression
Biochim. Biophys. Acta
1853
522-534
2015
Homo sapiens (O95453), Homo sapiens
Niedzwiecka, A.; Nilsson, P.; Worch, R.; Stepinski, J.; Darzynkiewicz, E.; Virtanen, A.
Molecular recognition of mRNA 5' cap by 3' poly(A)-specific ribonuclease (PARN) differs from interactions known for other cap-binding proteins
Biochim. Biophys. Acta
1864
331-345
2016
Homo sapiens (O95453)
Jadhav, G.; Kaur, I.; Maryati, M.; Airhihen, B.; Fischer, P.; Winkler, G.
Discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1
Bioorg. Med. Chem. Lett.
25
4219-4224
2015
Homo sapiens (O95453), Homo sapiens (Q9UIV1), Homo sapiens
Dhanraj, S.; Gunja, S.M.; Deveau, A.P.; Nissbeck, M.; Boonyawat, B.; Coombs, A.J.; Renieri, A.; Mucciolo, M.; Marozza, A.; Buoni, S.; Turner, L.; Li, H.; Jarrar, A.; Sabanayagam, M.; Kirby, M.; Shago, M.; Pinto, D.; Berman, J.N.; Scherer, S.W.; Virtanen, A.; Dror, Y.
Bone marrow failure and developmental delay caused by mutations in poly(A)-specific ribonuclease (PARN)
J. Med. Genet.
52
738-748
2015
Homo sapiens (O95453), Homo sapiens
Maragozidis, P.; Papanastasi, E.; Scutelnic, D.; Totomi, A.; Kokkori, I.; Zarogiannis, S.G.; Kerenidi, T.; Gourgoulianis, K.I.; Balatsos, N.A.
Poly(A)-specific ribonuclease and Nocturnin in squamous cell lung cancer prognostic value and impact on gene expression
Mol. Cancer
14
187
2015
Homo sapiens (O95453), Homo sapiens
Moon, D.H.; Segal, M.; Boyraz, B.; Guinan, E.; Hofmann, I.; Cahan, P.; Tai, A.K.; Agarwal, S.
Poly(A)-specific ribonuclease (PARN) mediates 3'-end maturation of the telomerase RNA component
Nat. Genet.
47
1482-1488
2015
Homo sapiens (O95453), Homo sapiens
Anastasakis, D.; Skeparnias, I.; Shaukat, A.N.; Grafanaki, K.; Kanellou, A.; Taraviras, S.; Papachristou, D.J.; Papakyriakou, A.; Stathopoulos, C.
Mammalian PNLDC1 is a novel poly(A) specific exonuclease with discrete expression during early development
Nucleic Acids Res.
44
8908-8920
2016
Homo sapiens (Q8NA58), Homo sapiens, Mus musculus (B2RXZ1), Mus musculus
Ishikawa, H.; Yoshikawa, H.; Izumikawa, K.; Miura, Y.; Taoka, M.; Nobe, Y.; Yamauchi, Y.; Nakayama, H.; Simpson, R.J.; Isobe, T.; Takahashi, N.
Poly(A)-specific ribonuclease regulates the processing of small-subunit rRNAs in human cells
Nucleic Acids Res.
45
3437-3447
2017
Homo sapiens (O95453), Homo sapiens
Montellese, C.; Montel-Lehry, N.; Henras, A.K.; Kutay, U.; Gleizes, P.E.; ODonohue, M.F.
Poly(A)-specific ribonuclease is a nuclear ribosome biogenesis factor involved in human 18S rRNA maturation
Nucleic Acids Res.
45
6822-6836
2017
Homo sapiens (O95453), Homo sapiens
Lee, D.; Park, D.; Park, J.; Kim, J.; Shin, C.
Poly(A)-specific ribonuclease sculpts the 3' ends of microRNAs
RNA
25
388-405
2019
Homo sapiens (O95453)
-
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