3.1.13.1: exoribonuclease II
This is an abbreviated version!
For detailed information about exoribonuclease II, go to the full flat file.
Word Map on EC 3.1.13.1
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3.1.13.1
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dnase
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nucleic
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pancreatic
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strand
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single-stranded
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endoribonuclease
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viruses
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polynucleotide
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endonuclease
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polyadenylation
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duplex
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polya
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ribonucleoproteins
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transcriptase
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rna-binding
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circrnas
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exosome
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phosphorylase
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chemokine
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dsrnas
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tata
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virion
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rpa
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nucleases
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stem-loops
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actinomycin
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helicase
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endonucleolytic
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dicer
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phosphodiester
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rna-dependent
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pronase
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intermedius
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oligoadenylate
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riboprobes
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rna-protein
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nucleolar
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ribozyme
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3'-terminal
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angiogenin
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argonaute
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encapsidation
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rna-induced
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pre-rrnas
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rna-dna
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antitoxin
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mip-1alpha
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snrnp
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medicine
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drosha
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degradation
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analysis
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norovirus
- 3.1.13.1
- dnase
- nucleic
- pancreatic
- strand
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single-stranded
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endoribonuclease
- viruses
- polynucleotide
- endonuclease
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polyadenylation
- duplex
- polya
- ribonucleoproteins
- transcriptase
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rna-binding
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circrnas
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exosome
- phosphorylase
- chemokine
- dsrnas
- tata
- virion
- rpa
- nucleases
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stem-loops
- actinomycin
- helicase
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endonucleolytic
- dicer
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phosphodiester
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rna-dependent
- pronase
- intermedius
- oligoadenylate
-
riboprobes
-
rna-protein
-
nucleolar
-
ribozyme
-
3'-terminal
-
angiogenin
-
argonaute
-
encapsidation
-
rna-induced
- pre-rrnas
- rna-dna
- antitoxin
-
mip-1alpha
-
snrnp
- medicine
- drosha
- degradation
- analysis
- norovirus
Reaction
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =
Synonyms
3'-5'exoribonuclease, 3’-5’exoribonuclease, 5'->3' exoribonuclease 2, AB205_0003320, Dis, Dis3, EC 3.1.4.20, exonuclease ISG20, More, PfRNase II, RC-RNase 2, ribonuclease 2, ribonuclease II, ribonuclease Q, Ribonuclease R, RNase, RNase 2, RNase A, RNase II, RNase R, RNase-2, RNaseR, Rnb, RNR, RNR1, Rrp44, XRN2
ECTree
3.1.13.1 exoribonuclease IIAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.1.13.1 - exoribonuclease II
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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
tRNAiMet + H2O
?
complete degradation of the hypomodified tRNA requires both Rrp44 and the poly(A) polymerase activity of TRAMP. The intact exosome lacking only the catalytic activity of Rrp44 fails to degrade tRNAi Met, showing this to be a specific Rrp44 substrate
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?
additional information
?
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the enzyme is involed in processing of polycistronic tRNA transcripts. Polynucleotide phosphorylase (PNPase) and RNase II are required for the removal of the 3Â’ Rho-dependent terminator sequences
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?
additional information
?
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RNase II is one of the major enzymes involved in mRNA processing. If the CSD is limiting the action of RNase II in vivo, it may play an important role working as a brake and thus preventing the massive degradation of RNA
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?
additional information
?
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-
RNase II degrades RNA hydrolytically in the 3' to 5' direction in a processive and sequence independent manner. RNase II activity is impaired by double-stranded RNAs
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?
additional information
?
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RNase II is a hydrolytic exoribonuclease that processively degrades RNA in the 3'-5' direction, is sensitive to secondary structures, it is also known to stall before it reaches a double-stranded region. Although RNase II degrading activity is sequence-independent, its favourite substrate is poly(A) tails. RNase II rapidly degrades poly (A) tails, but it halts if it finds secondary structures such as the Rho-independent terminators. The degradation of polyadenylated stretches by RNase II can paradoxically protect some RNAs because the other exoribonucleases (PNPase and RNase R) need a short poly(A) tail as a toehold in order to degrade secondary structures
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?
additional information
?
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RNase II is a hydrolytic exoribonuclease that processively degrades RNA in the 3'-5' direction, is sensitive to secondary structures, it is also known to stall before it reaches a double-stranded region. Although RNase II degrading activity is sequence-independent, its favourite substrate is poly(A) tails. RNase II rapidly degrades poly (A) tails, but it halts if it finds secondary structures such as the Rho-independent terminators. The degradation of polyadenylated stretches by RNase II can paradoxically protect some RNAs because the other exoribonucleases (PNPase and RNase R) need a short poly(A) tail as a toehold in order to degrade secondary structures
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?
additional information
?
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-
RNase II is a hydrolytic exoribonuclease that processively degrades RNA in the 3'-5' direction, is sensitive to secondary structures, it is also known to stall before it reaches a double-stranded region. Although RNase II degrading activity is sequence-independent, its favourite substrate is poly(A) tails. RNase II rapidly degrades poly (A) tails, but it halts if it finds secondary structures such as the Rho-independent terminators. The degradation of polyadenylated stretches by RNase II can paradoxically protect some RNAs because the other exoribonucleases (PNPase and RNase R) need a short poly(A) tail as a toehold in order to degrade secondary structures
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?
additional information
?
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RNase R is a hydrolytic exoribonuclease that processively degrades RNA in the 3'-5' direction. RNase R can easily degrade highly structured RNAs, but requires a single stranded region in order to be able to bind to the substrates. It was shown to be a key enzyme involved in the degradation of polyadenylated RNA
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?
additional information
?
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RNase R is a hydrolytic exoribonuclease that processively degrades RNA in the 3'-5' direction. RNase R can easily degrade highly structured RNAs, but requires a single stranded region in order to be able to bind to the substrates. It was shown to be a key enzyme involved in the degradation of polyadenylated RNA
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-
?
additional information
?
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-
RNase R is a hydrolytic exoribonuclease that processively degrades RNA in the 3'-5' direction. RNase R can easily degrade highly structured RNAs, but requires a single stranded region in order to be able to bind to the substrates. It was shown to be a key enzyme involved in the degradation of polyadenylated RNA
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-
?
additional information
?
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-
RNase II is one of the major enzymes involved in mRNA processing. If the CSD is limiting the action of RNase II in vivo, it may play an important role working as a brake and thus preventing the massive degradation of RNA
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-
?
additional information
?
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interactions between NKRF, 5'->3' exoribonuclease 2 (XRN2) and the negative elongation factor (NELF)-E in HeLa cells
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?
additional information
?
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at optimal (37°C) or elevated (42°C) growth temperatures, the loss of RNase R in the RNase R mutant has no major consequence on bacterial growth and has a moderate impact on normal gene regulation. At lower temperatures (25°C or 30°C), the loss of RNase R has a significant impact on bacterial growth and results in the accumulation of structured RNA degradation products. Concurrently, gene regulation is affected and specifically results in an increased expression of the competence regulon. Loss of the exoribonuclease activity of RNase R is sufficient to induce competence development, a genetically programmed process normally triggered as a response to environmental stimuli. The temperature-dependent expression of competence genes in the rnr mutant is independent of previously identified competence regulators. The rnr mutant is competent for genetic transformation. RNase R is dispensable for the intracellular multiplication of Legionella pneumophila in both human and protozoan hosts. A physiological role of RNase R is to eliminate structured RNA molecules that are stabilized by low temperature, which in turn may affect regulatory networks, compromising adaptation to cold and thus resulting in decreased viability
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?
additional information
?
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at optimal (37°C) or elevated (42°C) growth temperatures, the loss of RNase R in the RNase R mutant has no major consequence on bacterial growth and has a moderate impact on normal gene regulation. At lower temperatures (25°C or 30°C), the loss of RNase R has a significant impact on bacterial growth and results in the accumulation of structured RNA degradation products. Concurrently, gene regulation is affected and specifically results in an increased expression of the competence regulon. Loss of the exoribonuclease activity of RNase R is sufficient to induce competence development, a genetically programmed process normally triggered as a response to environmental stimuli. The temperature-dependent expression of competence genes in the rnr mutant is independent of previously identified competence regulators. The rnr mutant is competent for genetic transformation. RNase R is dispensable for the intracellular multiplication of Legionella pneumophila in both human and protozoan hosts. A physiological role of RNase R is to eliminate structured RNA molecules that are stabilized by low temperature, which in turn may affect regulatory networks, compromising adaptation to cold and thus resulting in decreased viability
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?
additional information
?
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the base preference for RNase 2 is UpG
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?
additional information
?
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the base preference for RNase 2 is UpG
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?
additional information
?
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mRNA is a direct substrate for RNase R
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?
additional information
?
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RNase R is a 3'-5'-exoribonuclease that is very processive and can efficiently digest RNAs having extensive secondary structures, such as rRNA, RNAs containing repetitive extragenic palindromic (REP) sequences, or the transfer-messenger RNA required for trans-translation.
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?
additional information
?
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RNase R is a 3'-5'-exoribonuclease that is very processive and can efficiently digest RNAs having extensive secondary structures, such as rRNA, RNAs containing repetitive extragenic palindromic (REP) sequences, or the transfer-messenger RNA required for trans-translation.
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?
additional information
?
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RNase R is also involved in the processing of 16S and 5S rRNA
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?
additional information
?
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RNase R is also involved in the processing of 16S and 5S rRNA
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?
additional information
?
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The absence of RNase R leads to moderate increases in the mRNA levels of some RNases and RNA helicases, but other RNases and RNA helicases are not affected.
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?
additional information
?
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The absence of RNase R leads to moderate increases in the mRNA levels of some RNases and RNA helicases, but other RNases and RNA helicases are not affected.
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-
?
additional information
?
-
mRNA is a direct substrate for RNase R
-
-
?
additional information
?
-
RNase R is a 3'-5'-exoribonuclease that is very processive and can efficiently digest RNAs having extensive secondary structures, such as rRNA, RNAs containing repetitive extragenic palindromic (REP) sequences, or the transfer-messenger RNA required for trans-translation.
-
-
?
additional information
?
-
RNase R is also involved in the processing of 16S and 5S rRNA
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-
?
additional information
?
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The absence of RNase R leads to moderate increases in the mRNA levels of some RNases and RNA helicases, but other RNases and RNA helicases are not affected.
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?
additional information
?
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Dis3 is responsible for exosome core activity
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?
additional information
?
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RNase activity of Dis3 is required for proper kinetochore formation and establishment of kinetochore-microtubule interactions. Dis3 is suggested to contribute to kinetochore formation through an involvement in heterochromatic silencing at both outer centromeric repeats and within the central core region
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?
additional information
?
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RNase activity of Dis3 is required for proper kinetochore formation and establishment of kinetochore-microtubule interactions. Dis3 is suggested to contribute to kinetochore formation through an involvement in heterochromatic silencing at both outer centromeric repeats and within the central core region
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?
