| http://purl.uniprot.org/citations/18657510 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18657510 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18657510 | http://www.w3.org/2000/01/rdf-schema#comment | "Helicases unwind duplex DNA ahead of the polymerases at the replication fork. However, the identity of the eukaryotic replicative helicase has been controversial; in vivo studies implicate the ring-shaped heterohexameric Mcm2-7 complex, although only a specific subset of Mcm subunits (Mcm467) unwind DNA in vitro. To address this discrepancy, we have compared both Mcm assemblies and find that they differ in their linear single-stranded DNA association rate and their ability to bind circular single-stranded DNA. These differences depend upon the Mcm2/5 interface, which we hypothesize serves as an ATP-dependent "gate" within Mcm2-7. Importantly, we find that reaction conditions that putatively close the Mcm2-7 "gate" reconstitute Mcm2-7 helicase activity. Unlike Mcm467, Mcm2-7 helicase activity is strongly anion dependent. Our results show that purified Mcm2-7 acts as a helicase, provides functional evidence of a Mcm2/5 gate, and lays the foundation for future mechanistic studies of this critical factor."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2008.05.020"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2008.05.020"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/author | "Bochman M.L."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/author | "Bochman M.L."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/author | "Schwacha A."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/author | "Schwacha A."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/pages | "287-293"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/pages | "287-293"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/title | "The Mcm2-7 complex has in vitro helicase activity."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/title | "The Mcm2-7 complex has in vitro helicase activity."xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/volume | "31"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://purl.uniprot.org/core/volume | "31"xsd:string |
| http://purl.uniprot.org/citations/18657510 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18657510 |
| http://purl.uniprot.org/citations/18657510 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18657510 |
| http://purl.uniprot.org/citations/18657510 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18657510 |
| http://purl.uniprot.org/citations/18657510 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18657510 |
| http://purl.uniprot.org/uniprot/P38132 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18657510 |
| http://purl.uniprot.org/uniprot/P30665 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18657510 |