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http://purl.uniprot.org/citations/24486609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24486609http://www.w3.org/2000/01/rdf-schema#comment"In a widely accepted model, the steroid receptor RNA activator protein (SRA protein; SRAP) modulates the transcriptional regulatory activity of SRA RNA by binding a specific stem-loop of SRA. We first confirmed that SRAP is present in the nucleus as well as the cytoplasm of MCF-7 breast cancer cells, where it is expressed at the level of about 10(5) molecules per cell. However, our SRAP-RNA binding experiments, both in vitro with recombinant protein and in cultured cells with plasmid-expressed protein and RNA, did not reveal a specific interaction between SRAP and SRA. We determined the crystal structure of the carboxy-terminal domain of human SRAP and found that it does not have the postulated RRM (RNA recognition motif). The structure is a five-helix bundle that is distinct from known RNA-binding motifs and instead is similar to the carboxy-terminal domain of the yeast spliceosome protein PRP18, which stabilizes specific protein-protein interactions within a multisubunit mRNA splicing complex. SRA binding experiments with this domain gave negative results. Transcriptional regulation by SRA/SRAP was examined with siRNA knockdown. Effects on both specific estrogen-responsive genes and genes identified by RNA-seq as candidates for regulation were examined in MCF-7 cells. Only a small effect (~20% change) on one gene resulting from depletion of SRA/SRAP could be confirmed. We conclude that the current model for SRAP function must be reevaluated; we suggest that SRAP may function in a different context to stabilize specific intermolecular interactions in the nucleus."xsd:string
http://purl.uniprot.org/citations/24486609http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2014.01.006"xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/author"Cech T.R."xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/author"McKay D.B."xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/author"Xi L."xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/author"Barthel K.K.B."xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/pages"1766-1785"xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/title"Structure and function of steroid receptor RNA activator protein, the proposed partner of SRA noncoding RNA."xsd:string
http://purl.uniprot.org/citations/24486609http://purl.uniprot.org/core/volume"426"xsd:string
http://purl.uniprot.org/citations/24486609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24486609
http://purl.uniprot.org/citations/24486609http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24486609
http://purl.uniprot.org/uniprot/Q9HD15#attribution-2A2B4C9B724358588B71B7FB72F0DEA9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24486609
http://purl.uniprot.org/uniprot/Q9HD15#attribution-3F6CC1332156E73FA2EF07B3EC3A5128http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24486609
http://purl.uniprot.org/uniprot/#_B3KNT3-mappedCitation-24486609http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24486609
http://purl.uniprot.org/uniprot/#_Q9HD15-mappedCitation-24486609http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24486609
http://purl.uniprot.org/uniprot/Q9HD15http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24486609
http://purl.uniprot.org/uniprot/B3KNT3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24486609