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http://purl.uniprot.org/citations/17053788http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17053788http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17053788http://www.w3.org/2000/01/rdf-schema#comment"SMG6 and SMG5 are essential factors in nonsense-mediated mRNA decay, a conserved pathway that degrades mRNAs with premature translation termination codons. Both SMG5 and SMG6 have been predicted to contain a C-terminal PIN (PilT N-terminus) domain, present in proteins with ribonuclease activity. We have determined the structures of human SMG5 and SMG6 PIN domains. Although they share a similar overall fold related to ribonucleases of the RNase H family, they have local differences at the putative active site. SMG6 has the canonical triad of acidic residues that are crucial in RNase H for nuclease activity, while SMG5 lacks key catalytic residues. The structural differences are reflected at the functional level. Only the PIN domain of SMG6 has degradation activity on single-stranded RNA in vitro. This difference in catalytic activity is conserved in Drosophila, where an SMG6 with an inactive PIN domain inhibits NMD in a dominant-negative manner. Our findings suggest that the NMD machinery has intrinsic nuclease activity that is likely to contribute to the rapid decay of mRNAs that terminate translation prematurely."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601377"xsd:string
http://purl.uniprot.org/citations/17053788http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601377"xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Izaurralde E."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Izaurralde E."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Conti E."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Conti E."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Behm-Ansmant I."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Behm-Ansmant I."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Glavan F."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/author"Glavan F."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/pages"5117-5125"xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/pages"5117-5125"xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/title"Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/title"Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex."xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/17053788http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/17053788http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17053788
http://purl.uniprot.org/citations/17053788http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17053788