ArticleThe Journal of biological chemistry2008
Multiple mechanisms contribute to Schizosaccharomyces pombe origin recognition complex-DNA interactions.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 34 citations in OpenAlex.
- The origin recognition complex requires chromatin tethering by a hypervariable intrinsically disordered region that is functionally conserved from sponge to man.Nucleic acids research · 2024Article
- Structural insight into the assembly and conformational activation of human origin recognition complex.Cell discovery · 2020Article
- Molecular mechanisms of eukaryotic origin initiation, replication fork progression, and chromatin maintenance.The Biochemical journal · 2020Article
- A new class of disordered elements controls DNA replication through initiator self-assembly.eLife · 2019Article
- 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
- 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
- Specific binding of eukaryotic ORC to DNA replication origins depends on highly conserved basic residues.Scientific reports · 2015Article
- Article
- Geminin inhibits a late step in the formation of human pre-replicative complexes.The Journal of biological chemistry · 2014Article
- Origin licensing requires ATP binding and hydrolysis by the MCM replicative helicase.Molecular cell · 2014Article
- Activation of a human chromosomal replication origin by protein tethering.Nucleic acids research · 2013Article
- Helicase loading at chromosomal origins of replication.Cold Spring Harbor perspectives in biology · 2013Review
- Helicobacter pylori oriC--the first bipartite origin of chromosome replication in Gram-negative bacteria.Nucleic acids research · 2012Article
- Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy.Structure (London, England : 1993) · 2012Article
- The origin recognition complex: a biochemical and structural view.Sub-cellular biochemistry · 2012Review
- Article
- Novel features of ARS selection in budding yeast Lachancea kluyveri.BMC genomics · 2011Article
- Human initiation protein Orc4 prefers triple stranded DNA.Molecular biology reports · 2010Article
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7 authors at 1 institution in 1 country.
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Abstract
Eukaryotic DNA replication requires the assembly of multiprotein pre-replication complexes (pre-RCs) at chromosomal origins of DNA replication. Here we describe the interactions of highly purified Schizosaccharomyces pombe pre-RC components, SpORC, SpCdc18, and SpCdt1, with each other and with ars1 origin DNA. We show that SpORC binds DNA in at least two steps. The first step likely involves electrostatic interactions between the AT-hook motifs of SpOrc4 and AT tracts in ars1 DNA and results in the formation of a salt-sensitive complex. In the second step, the salt-sensitive complex is slowly converted to a salt-stable complex that involves additional interactions between SpORC and DNA. Binding of SpORC to ars1 DNA is facilitated by negative supercoiling and is accompanied by changes in DNA topology, suggesting that SpORC-DNA complexes contain underwound or negatively writhed DNA. Purified human origin recognition complex (ORC) induces similar topological changes in origin DNA, indicating that this property of ORC is conserved in eukaryotic evolution and plays an important role in ORC function. We also show that SpCdc18 and SpCdt1 form a binary complex that has greater affinity for DNA than either protein alone. In addition, both proteins contribute significantly to the stability of the initial SpORC-DNA complex and enhance the SpORC-dependent topology changes in origin DNA. Thus, the formation of stable protein-DNA complexes at S. pombe origins of replication involves binary interactions among all three proteins, as well as interactions of both SpORC and SpCdt1-SpCdc18 with origin DNA. These findings demonstrate that SpORC is not the sole determinant of origin recognition.
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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.