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18S-E pre-rRNA + H2O
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miR-362-5p + H2O
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miR-362-5p is defined by DROSHA and DICER to 26 nt in length
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mRNA-poly(A) + H2O
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the enzyme is involved in the removal of polyA tails from mRNAs
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poly(A) RNA + H2O
5'-AMP + ?
poly(A)-mRNA + H2O
5'-AMP
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additional information
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poly(A) RNA + H2O
5'-AMP + ?
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poly(A) RNA + H2O
5'-AMP + ?
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no activity on poly(U), poly(C), 23rRNA
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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)
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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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poly(A) RNA + H2O
5'-AMP + ?
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poly(A) RNA + H2O
5'-AMP + ?
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deadenylation of mRNA
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poly(A) RNA + H2O
5'-AMP + ?
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poly(A) RNA + H2O
5'-AMP + ?
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poly(A) RNA + H2O
5'-AMP + ?
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additional information
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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
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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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physiological role of enzyme, recognition mechanisms that target mRNA for degradation
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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
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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
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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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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
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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
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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
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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
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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
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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
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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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mRNA deadenylation by exoribonucleolytic activity of PARN is not essential for embryogenesis and viability
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