http://purl.uniprot.org/citations/17543985 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17543985 | http://www.w3.org/2000/01/rdf-schema#comment | "N Oct-3, a transcription factor member of the POU protein family, is implicated in normal central nervous system development but also in melanoma growth. Its DNA-binding domain (DBD) comprises two subdomains, POUs and POUh, joined by a linker peptide. We have previously shown that N Oct-3 can interact with the already described PORE and MORE DNA motifs, but also with a new structural element we have termed NORE. Having observed that both the PORE and NORE DNA-association modes depend on a strong anchoring of the POUh subdomain rigid arm into the DNA-target minor groove, in contrast to the MORE mode, we have formulated the hypothesis that phosphorylation of the conserved Ser101 residue located in the N Oct-3 POUh arm could lead to differential results in DNA binding according to the type of target. Here we demonstrate that, in vitro, Ser101 is phosphorylated by protein kinase A (PKA), either purified or contained in melanoma (624 mel) nuclear extract, and that this phosphorylation indeed significantly reduced N Oct-3 DBD binding to PORE and NORE motifs, most likely by hampering the POUh rigid arm insertion in the DNA minor groove. Conversely, no effect was observed on the binding of N Oct-3 DBD to MORE sequences. Finally, once bound to its DNA targets, N Oct-3 DBD is less susceptible to PKA activity. We conclude that transcription of genes exhibiting a MORE motif in their promoter should be less affected by N Oct-3 phosphorylation than that of genes switched on by PORE or NORE sequences."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2007.04.072"xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Stella A."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Erard M."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Burlet-Schiltz O."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Monsarrat B."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Clottes E."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Henri P."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Nieto L."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/author | "Joseph G."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/pages | "687-700"xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/title | "Differential effects of phosphorylation on DNA binding properties of N Oct-3 are dictated by protein/DNA complex structures."xsd:string |
http://purl.uniprot.org/citations/17543985 | http://purl.uniprot.org/core/volume | "370"xsd:string |
http://purl.uniprot.org/citations/17543985 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17543985 |
http://purl.uniprot.org/citations/17543985 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17543985 |
http://purl.uniprot.org/uniprot/#_P20265-mappedCitation-17543985 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17543985 |
http://purl.uniprot.org/uniprot/P20265 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/17543985 |