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http://purl.uniprot.org/citations/11823439http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11823439http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11823439http://www.w3.org/2000/01/rdf-schema#comment"We report that the cyclophilin USA-CyP is part of distinct complexes with two spliceosomal proteins and is involved in both steps of pre-mRNA splicing. The splicing factors hPrp18 and hPrp4 have a short region of homology that defines a high affinity binding site for USA-CyP in each protein. USA-CyP forms separate, stable complexes with hPrp18 and hPrp4 in which the active site of the cyclophilin is exposed. The cyclophilin inhibitor cyclosporin A slows pre-mRNA splicing in vitro, and we show that its inhibition of the second step of splicing is caused by blocking the action of USA-CyP within its complex with hPrp18. Cyclosporin A also slows splicing in vivo, and we show that this slowing results specifically from inhibition of USA-CyP. Our results lead to a model in which USA-CyP is carried into the spliceosome in complexes with hPrp4 and hPrp18, and USA-CyP acts during splicing within these complexes. These results provide an example of the function of a cyclophilin in a complex process and provide insight into the mechanisms of action of cyclophilins."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.org/dc/terms/identifier"doi:10.1093/emboj/21.3.470"xsd:string
http://purl.uniprot.org/citations/11823439http://purl.org/dc/terms/identifier"doi:10.1093/emboj/21.3.470"xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Lee E.J."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Lee E.J."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Misteli T."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Misteli T."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Horowitz D.S."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Horowitz D.S."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Mabon S.A."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/author"Mabon S.A."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/pages"470-480"xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/pages"470-480"xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/title"A cyclophilin functions in pre-mRNA splicing."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/title"A cyclophilin functions in pre-mRNA splicing."xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/11823439http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/11823439http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11823439
http://purl.uniprot.org/citations/11823439http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11823439