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http://purl.uniprot.org/citations/15024032http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15024032http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15024032http://www.w3.org/2000/01/rdf-schema#comment"We present a new in vitro system for characterizing the binding and mobility of enhanced green fluorescent protein (EGFP)-labeled nuclear proteins by fluorescence recovery after photobleaching in digitonin-permeabilized cells. This assay reveals that SRm160, a splicing coactivator and component of the exon junction complex (EJC) involved in RNA export, has an adenosine triphosphate (ATP)-dependent mobility. Endogenous SRm160, lacking the EGFP moiety, could also be released from sites at splicing speckled domains by an ATP-dependent mechanism. A second EJC protein, RNPS1, also has an ATP-dependent mobility, but SRm300, a protein that binds to SRm160 and participates with it in RNA splicing, remains immobile after ATP supplementation. This finding suggests that SRm160-containing RNA export, but not splicing, complexes have an ATP-dependent mobility. We propose that RNA export complexes have an ATP-regulated mechanism for release from binding sites at splicing speckled domains. In vitro fluorescence recovery after photobleaching is a powerful tool for identifying cofactors required for nuclear binding and mobility."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200307002"xsd:string
http://purl.uniprot.org/citations/15024032http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200307002"xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Wagner S."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Wagner S."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Ivshina M."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Ivshina M."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Nickerson J.A."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Nickerson J.A."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Chiosea S."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/author"Chiosea S."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/pages"843-850"xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/pages"843-850"xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/title"In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/title"In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon junction complex protein SRm160."xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/volume"164"xsd:string
http://purl.uniprot.org/citations/15024032http://purl.uniprot.org/core/volume"164"xsd:string
http://purl.uniprot.org/citations/15024032http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15024032
http://purl.uniprot.org/citations/15024032http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15024032