| http://purl.uniprot.org/citations/1406630 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1406630 | http://www.w3.org/2000/01/rdf-schema#comment | "Analysis of the p50 and p65 subunits of the NF-kappa B transcription factor complex has revealed that both proteins can interact with related DNA sequences through either homo- or heterodimer formation. In addition, the product of the proto-oncogene c-rel can bind to similar DNA motifs by itself or as a heterodimer with p50 or p65. However, these studies have used a limited number of known kappa B DNA motifs, and the question of the optimal DNA sequences preferred by each homodimer has not been addressed. Using purified recombinant p50, p65, and c-Rel proteins, optimal DNA-binding motifs were selected from a pool of random oligonucleotides. Alignment of the selected sequences allowed us to predict a consensus sequence for binding of the individual homodimeric Rel-related proteins, and DNA-protein binding analysis of the selected DNA sequences revealed sequence specificity of the proteins. Contrary to previous assumptions, we observed that p65 homodimers can interact with a subset of DNA sequences not recognized by p50 homodimers. Differential binding affinities were also obtained with p50- and c-Rel-selected sequences. Using either a p50- or p65-selected kappa B motif, which displayed differential binding with respect to the other protein, little to no binding was observed with the heterodimeric NF-kappa B complex. Similarly, in transfection experiments in which the selective kappa B binding sites were used to drive the expression of a chloramphenicol acetyltransferase reporter construct, the p65- and p50-selected motifs were activated only in the presence of p65 and p50/65 (a chimeric protein with the p50 DNA binding domain and p65 activation domain) expression vectors, respectively, and neither demonstrated a significant response to stimuli that induce NF-kappa B activity. These findings demonstrate that interaction of both subunits of the heterodimeric NF-kappa B complex with DNA is required for DNA binding and transcriptional activation and suggest that transcriptional activation mediated by the individual rel-related proteins will differ dramatically, depending on the specific kappa B motifs present."xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.12.10.4412-4421.1992"xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/author | "Kunsch C."xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/author | "Rosen C.A."xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/author | "Ruben S.M."xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/pages | "4412-4421"xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/title | "Selection of optimal kappa B/Rel DNA-binding motifs: interaction of both subunits of NF-kappa B with DNA is required for transcriptional activation."xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/1406630 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1406630 |
| http://purl.uniprot.org/citations/1406630 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1406630 |
| http://purl.uniprot.org/uniprot/P19838#attribution-B11685B6150148F7ED8864BBE5FFD3B8 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1406630 |
| http://purl.uniprot.org/uniprot/Q04864#attribution-B11685B6150148F7ED8864BBE5FFD3B8 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1406630 |
| http://purl.uniprot.org/uniprot/Q04206#attribution-774B219DAEC531844C9D9E545B614CF9 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1406630 |
| http://purl.uniprot.org/uniprot/Q04206#attribution-B11685B6150148F7ED8864BBE5FFD3B8 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/1406630 |