ArticleStructure (London, England : 1993)2012
Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 71 citations in OpenAlex.
- An Orc1 initiator-specific motif (ISM)-related region limits ORC-ssDNA binding and promotes replication origin specificity in budding yeast.Frontiers in microbiology · 2026Article
- Reconstitution of human DNA licensing and the structural and functional analysis of key intermediates.Nature communications · 2025Article
- Four decades of Eukaryotic DNA replication: From yeast genetics to high-resolution cryo-EM structures of the replisome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ordered and disordered regions of the Origin Recognition Complex direct differential in vivo binding at distinct motif sequences.Nucleic acids research · 2024Article
- An essential Noc3p dimerization cycle mediates ORC double-hexamer formation in replication licensing.Life science alliance · 2023Article
- DNA Replication Licensing Factors: Novel Targets for Cancer Therapy via Inhibiting the Stemness of Cancer Cells.International journal of biological sciences · 2022Review
- Replication initiation: Implications in genome integrity.DNA repair · 2021Review
- Investigation of the Interaction of Human Origin Recognition Complex Subunit 1 with G-Quadruplex DNAs of HumanInternational journal of molecular sciences · 2021Article
- Pax3 inhibits Neuro-2a cells proliferation and neurite outgrowth.Journal of cellular and molecular medicine · 2021Article
- The dynamic nature of the human origin recognition complex revealed through five cryoEM structures.eLife · 2020Article
- Evolution of metabolic capabilities and molecular features of diplonemids, kinetoplastids, and euglenids.BMC biology · 2020Article
- Investigating Tunneling Nanotubes in Cancer Cells: Guidelines for Structural and Functional Studies through Cell Imaging.BioMed research international · 2020Review
- Changing Perspectives on the Role of DnaA-ATP in Orisome Function and Timing Regulation.Frontiers in microbiology · 2019Review
- Origin recognition is the predominant role for DnaA-ATP in initiation of chromosome replication.Nucleic acids research · 2018Article
- Conformational control and DNA-binding mechanism of the metazoan origin recognition complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conservation and Variation in Strategies for DNA Replication of Kinetoplastid Nuclear Genomes.Current genomics · 2018Review
- Collective helicity switching of a DNA-coat assembly.Nature nanotechnology · 2017Article
- From structure to mechanism-understanding initiation of DNA replication.Genes & development · 2017Review
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- Structural basis of Mcm2-7 replicative helicase loading by ORC-Cdc6 and Cdt1.Nature structural & molecular biology · 2017Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.