ArticleJournal of structural biology2008
Single particle EM studies of the Drosophila melanogaster origin recognition complex and evidence for DNA wrapping.
Article in Journal of structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 33 citations in OpenAlex.
- Molecular mechanisms of eukaryotic origin initiation, replication fork progression, and chromatin maintenance.The Biochemical journal · 2020Article
- Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites.Nucleic acids research · 2020Article
- Origins of DNA replication.PLoS genetics · 2019Review
- 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
- DNA Replication Control DuringGenetics · 2017Review
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- Cryo-EM of dynamic protein complexes in eukaryotic DNA replication.Protein science : a publication of the Protein Society · 2017Review
- Diverged composition and regulation of the Trypanosoma brucei origin recognition complex that mediates DNA replication initiation.Nucleic acids research · 2016Article
- ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila.Nucleic acids research · 2016Article
- DNA sequence templates adjacent nucleosome and ORC sites at gene amplification origins in Drosophila.Nucleic acids research · 2015Article
- Article
- Cryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA.Nature structural & molecular biology · 2013Article
- Helicase loading at chromosomal origins of replication.Cold Spring Harbor perspectives in biology · 2013Review
- Mechanisms for initiating cellular DNA replication.Annual review of biochemistry · 2013Review
- Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy.Structure (London, England : 1993) · 2012Article
- The dynamics of replication licensing in live Caenorhabditis elegans embryos.The Journal of cell biology · 2012Article
- Article
- Different roles of the human Orc6 protein in the replication initiation process.Cellular and molecular life sciences : CMLS · 2011Article
- Structural analysis of human Orc6 protein reveals a homology with transcription factor TFIIB.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Conserved nucleosome positioning defines replication origins.Genes & development · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hyperphosphorylation of the Drosophila melanogaster origin recognition complex (DmORC) by cyclin dependent kinases (CDKs) allows nucleotide binding but inhibits the ATPase activity of Orc1, and ablates the ATP-dependent interaction of ORC with DNA. Here we present single particle electron microscopy (EM) studies of ORC bound to nucleotide in both the dephosphorylated and hyper-phosphorylated states. 3D image reconstructions show that nucleotide binding gives rise to an analogous conformation independent of phosphorylation state. At the intermediate resolution achieved in our studies, ATP promotes changes along the toroidal core of the complex with negligible differences contributed by phosphorylation. Thus, hyperphosphorylation of DmORC does not induce meso-scale rearrangement of the ORC structure. To better understand ORC's role in origin remodeling, we performed atomic force microscopy (AFM) studies that show the contour length of a 688bp linear DNA fragment shortens by the equivalent of approximately 130bp upon ORC binding. This data, coupled with previous studies that showed a linking number change in circular DNA upon ORC binding, suggests that ORC may wrap the DNA in a manner akin to DnaA. Based on existing data and our structures, we propose a subunit arrangement for the AAA+ and winged helix domains, and in addition, speculate on a path of the 133bp of DNA around the ORC complex.
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Registered trials
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.