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http://purl.uniprot.org/citations/21245038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21245038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21245038http://www.w3.org/2000/01/rdf-schema#comment"The vertebrate 2-5A system is part of the innate immune system and central to cellular antiviral defense. Upon activation by viral double-stranded RNA, 5'-triphosphorylated, 2'-5'-linked oligoadenylate polyribonucleotides (2-5As) are synthesized by one of several 2'-5'-oligoadenylate synthetases. These unusual oligonucleotides activate RNase L, an unspecific endoribonuclease that mediates viral and cellular RNA breakdown. Subsequently, the 2-5As are removed by a 2'-phosphodiesterase (2'-PDE), an enzyme that apart from breaking 2'-5' bonds also degrades regular, 3'-5'-linked oligoadenylates. Interestingly, 2'-PDE shares both functionally and structurally characteristics with the CCR4-type exonuclease-endonuclease-phosphatase family of deadenylases. Here we show that 2'-PDE locates to the mitochondrial matrix of human cells, and comprise an active 3'-5' exoribonuclease exhibiting a preference for oligo-adenosine RNA like canonical cytoplasmic deadenylases. Furthermore, we document a marked negative association between 2'-PDE and mitochondrial mRNA levels following siRNA-directed knockdown and plasmid-mediated overexpression, respectively. The results indicate that 2'-PDE, apart from playing a role in the cellular immune system, may also function in mitochondrial RNA turnover."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkq1282"xsd:string
http://purl.uniprot.org/citations/21245038http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkq1282"xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Andersen K.R."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Andersen K.R."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Talbo G.H."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Talbo G.H."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Hoogenraad N."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Hoogenraad N."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Brodersen D.E."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Brodersen D.E."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Vestergaard A.L."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Vestergaard A.L."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Faou P."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Faou P."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Justesen J."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Justesen J."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Martensen P.M."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Martensen P.M."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Kjaer K.H."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Kjaer K.H."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Poulsen J.B."xsd:string
http://purl.uniprot.org/citations/21245038http://purl.uniprot.org/core/author"Poulsen J.B."xsd:string