RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/24064211http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24064211http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24064211http://www.w3.org/2000/01/rdf-schema#comment"Geminin is an important regulator of proliferation and differentiation in metazoans, which predominantly inhibits the DNA replication licensing factor Cdt1, preventing genome over-replication. We show that Geminin preferentially forms stable coiled-coil heterodimers with its homologue, Idas. In contrast to Idas-Geminin heterodimers, Idas homodimers are thermodynamically unstable and are unlikely to exist as a stable macromolecule under physiological conditions. The crystal structure of the homology regions of Idas in complex with Geminin showed a tight head-to-head heterodimeric coiled-coil. This Idas-Geminin heterodimer binds Cdt1 less strongly than Geminin-Geminin, still with high affinity (∼30 nm), but with notably different thermodynamic properties. Consistently, in Xenopus egg extracts, Idas-Geminin is less active in licensing inhibition compared with a Geminin-Geminin homodimer. In human cultured cells, ectopic expression of Idas leads to limited over-replication, which is counteracted by Geminin co-expression. The properties of the Idas-Geminin complex suggest it as the functional form of Idas and provide a possible mechanism to modulate Geminin activity."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.491928"xsd:string
http://purl.uniprot.org/citations/24064211http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.491928"xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Perrakis A."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Perrakis A."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Caillat C."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Caillat C."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Blow J.J."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Blow J.J."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Lygerou Z."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Lygerou Z."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Taraviras S."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Taraviras S."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Gillespie P.J."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Gillespie P.J."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Pefani E.D."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/author"Pefani E.D."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/pages"31624-31634"xsd:string
http://purl.uniprot.org/citations/24064211http://purl.uniprot.org/core/pages"31624-31634"xsd:string