| Literature DB >> 22405012 |
Jingchuan Sun1, Hironori Kawakami, Juergen Zech, Christian Speck, Bruce Stillman, Huilin Li.
Abstract
The eukaryotic origin recognition complex (ORC) interacts with and remodels origins of DNA replication prior to initiation in S phase. Here, we report a single-particle cryo-EM-derived structure of the supramolecular assembly comprising Saccharomyces cerevisiae ORC, the replication initiation factor Cdc6, and double-stranded ARS1 origin DNA in the presence of ATPγS. The six subunits of ORC are arranged as Orc1:Orc4:Orc5:Orc2:Orc3, with Orc6 binding to Orc2. Cdc6 binding changes the conformation of ORC, in particular reorienting the Orc1 N-terminal BAH domain. Segmentation of the 3D map of ORC-Cdc6 on DNA and docking with the crystal structure of the homologous archaeal Orc1/Cdc6 protein suggest an origin DNA binding model in which the DNA tracks along the interior surface of the crescent-like ORC. Thus, ORC bends and wraps the DNA. This model is consistent with the observation that binding of a single Cdc6 extends the ORC footprint on origin DNA from both ends. Copyright ÂEntities:
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Year: 2012 PMID： 22405012 PMCID： PMC3299985 DOI： 10.1016/j.str.2012.01.011
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006