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http://purl.uniprot.org/citations/26779609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26779609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26779609http://www.w3.org/2000/01/rdf-schema#comment"The RNase XRN2 is essential in RNA metabolism. In Caenorhabditis elegans, XRN2 functions with PAXT-1, which shares a putative XRN2-binding domain (XTBD) with otherwise unrelated mammalian proteins. Here, we characterize the structure and function of an XTBD-XRN2 complex. Although XTBD stably interconnects two XRN2 domains through numerous interacting residues, mutation of a single critical residue suffices to disrupt XTBD-XRN2 complexes in vitro and to recapitulate paxt-1-null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (HsC2AIL) can substitute for PAXT-1 in vivo. In vertebrates, which express three distinct XTBD-containing proteins, XRN2 may partition into distinct stable heterodimeric complexes, which probably differ in subcellular localization or function. In C. elegans, complex formation with PAXT-1, the sole XTBD protein, serves to preserve the stability of XRN2 in the absence of substrate."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.3155"xsd:string
http://purl.uniprot.org/citations/26779609http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.3155"xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Gut H."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Gut H."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Richter H."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Richter H."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Grosshans H."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Grosshans H."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Katic I."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/author"Katic I."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/pages"164-171"xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/pages"164-171"xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/title"Structural basis and function of XRN2 binding by XTB domains."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/title"Structural basis and function of XRN2 binding by XTB domains."xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/26779609http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/26779609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26779609
http://purl.uniprot.org/citations/26779609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26779609