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http://purl.uniprot.org/citations/7862145http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7862145http://www.w3.org/2000/01/rdf-schema#comment"Alveolar rhabdomyosarcomas are pediatric solid tumors with a hallmark cytogenetic abnormality: translocation of chromosomes 2 and 13 [t(2;13) (q35;q14)]. The genes on each chromosome involved in this translocation have been identified as the transcription factor-encoding genes PAX3 and FKHR. The NH2-terminal paired box and homeodomain DNA-binding domains of PAX3 are fused in frame to COOH-terminal regions of the chromosome 13-derived FKHR gene, a novel member of the forkhead DNA-binding domain family. To determine the role of the fusion protein in transcriptional regulation and oncogenesis, we identified the PAX3-FKHR fusion protein and characterized its function(s) as a transcription factor relative to wild-type PAX3. Antisera specific to PAX3 and FKHR were developed and used to examine PAX3 and PAX3-FKHR expression in tumor cell lines. Sequential immunoprecipitations with anti-PAX3 and anti-FKHR sera demonstrated expression of a 97-kDa PAX3-FKHR fusion protein in the t(2;13)-positive rhabdomyosarcoma Rh30 cell line and verified that a single polypeptide contains epitopes derived from each protein. The PAX3-FKHR protein was localized to the nucleus in Rh30 cells, as was wild-type PAX3, in t(2;13)-negative A673 cells. In gel shift assays using a canonical PAX binding site (e5 sequence), we found that DNA binding of PAX3-FKHR was significantly impaired relative to that of PAX3 despite the two proteins having identical PAX DNA-binding domains. However, the PAX3-FKHR fusion protein was a much more potent transcriptional activator than PAX3 as determined by transient cotransfection assays using e5-CAT reporter plasmids. The PAX3-FKHR protein may function as an oncogenic transcription factor by enhanced activation of normal PAX3 target genes."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.org/dc/terms/identifier"doi:10.1128/mcb.15.3.1522"xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Mukhopadhyay S."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Fredericks W.J."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Rovera G."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Galili N."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Barr F.G."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Rauscher F.J."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/author"Bennicelli J."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/name"Mol Cell Biol"xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/pages"1522-1535"xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/title"The PAX3-FKHR fusion protein created by the t(2;13) translocation in alveolar rhabdomyosarcomas is a more potent transcriptional activator than PAX3."xsd:string
http://purl.uniprot.org/citations/7862145http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/7862145http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7862145
http://purl.uniprot.org/citations/7862145http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7862145
http://purl.uniprot.org/uniprot/Q12778#attribution-5C67A43AAAB27DC670E4BEB66230EAE3http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/7862145