| http://purl.uniprot.org/citations/22856882 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22856882 | http://www.w3.org/2000/01/rdf-schema#comment | "Crystal structures of the GCN4 bZIP (basic region/leucine zipper) with the AP-1 or CRE site show how each GCN4 basic region binds to a 4 bp cognate half-site as a single DNA target; however, this may not always fully describe how bZIP proteins interact with their target sites. Previously, we showed that the GCN4 basic region interacts with all 5 bp in half-site TTGCG (termed 5H-LR) and that 5H-LR comprises two 4 bp subsites, TTGC and TGCG, which individually are also target sites of the basic region. In this work, we explore how the basic region interacts with 5H-LR when the bZIP dimer localizes to full-sites. Using AMBER molecular modeling, we simulated GCN4 bZIP complexes with full-sites containing 5H-LR to investigate in silico the interface between the basic region and 5H-LR. We also performed in vitro investigation of bZIP-DNA interactions at a number of full-sites that contain 5H-LR versus either subsite: we analyzed results from DNase I footprinting and electrophoretic mobility shift assay (EMSA) and from EMSA titrations to quantify binding affinities. Our computational and experimental results together support a highly dynamic DNA-binding model: when a bZIP dimer localizes to its target full-site, the basic region can alternately recognize either subsite as a distinct target at 5H-LR and translocate between the subsites, potentially by sliding and hopping. This model provides added insights into how α-helical DNA-binding domains of transcription factors can localize to their gene regulatory sequences in vivo."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi300718f"xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/author | "Fedorova A.V."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/author | "Shin J.A."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/author | "Chan I.S."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/author | "Shahravan S.H."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/author | "Al-Sarraj T."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/pages | "6632-6643"xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/title | "The bZIP dimer localizes at DNA full-sites where each basic region can alternately translocate and bind to subsites at the half-site."xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://purl.uniprot.org/core/volume | "51"xsd:string |
| http://purl.uniprot.org/citations/22856882 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22856882 |
| http://purl.uniprot.org/citations/22856882 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22856882 |
| http://purl.uniprot.org/uniprot/#_P03069-mappedCitation-22856882 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22856882 |
| http://purl.uniprot.org/uniprot/P03069 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22856882 |