http://purl.uniprot.org/citations/28096349 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/28096349 | http://www.w3.org/2000/01/rdf-schema#comment | "The eukaryotic CMG (Cdc45, Mcm2-7, GINS) helicase consists of the Mcm2-7 hexameric ring along with five accessory factors. The Mcm2-7 heterohexamer, like other hexameric helicases, is shaped like a ring with two tiers, an N-tier ring composed of the N-terminal domains, and a C-tier of C-terminal domains; the C-tier contains the motor. In principle, either tier could translocate ahead of the other during movement on DNA. We have used cryo-EM single-particle 3D reconstruction to solve the structure of CMG in complex with a DNA fork. The duplex stem penetrates into the central channel of the N-tier and the unwound leading single-strand DNA traverses the channel through the N-tier into the C-tier motor, 5'-3' through CMG. Therefore, the N-tier ring is pushed ahead by the C-tier ring during CMG translocation, opposite the currently accepted polarity. The polarity of the N-tier ahead of the C-tier places the leading Pol ε below CMG and Pol α-primase at the top of CMG at the replication fork. Surprisingly, the new N-tier to C-tier polarity of translocation reveals an unforeseen quality-control mechanism at the origin. Thus, upon assembly of head-to-head CMGs that encircle double-stranded DNA at the origin, the two CMGs must pass one another to leave the origin and both must remodel onto opposite strands of single-stranded DNA to do so. We propose that head-to-head motors may generate energy that underlies initial melting at the origin."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1620500114"xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Li H."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Sun J."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Yuan Z."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Zhang D."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "O'Donnell M.E."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Bai L."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Yurieva O."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "Georgescu R."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/author | "de Luna Almeida Santos R."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/pages | "E697-E706"xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/title | "Structure of eukaryotic CMG helicase at a replication fork and implications to replisome architecture and origin initiation."xsd:string |
http://purl.uniprot.org/citations/28096349 | http://purl.uniprot.org/core/volume | "114"xsd:string |
http://purl.uniprot.org/citations/28096349 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28096349 |
http://purl.uniprot.org/citations/28096349 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/28096349 |
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http://purl.uniprot.org/uniprot/#_P24279-mappedCitation-28096349 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28096349 |
http://purl.uniprot.org/uniprot/#_P38132-mappedCitation-28096349 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28096349 |