ArticleScientific reports2015
Specific binding of eukaryotic ORC to DNA replication origins depends on highly conserved basic residues.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 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
- Ordered and disordered regions of the Origin Recognition Complex direct differential in vivo binding at distinct motif sequences.Nucleic acids research · 2024Article
- Origin recognition complex subunit 1(ORC1) is a potential biomarker and therapeutic target in cancer.BMC medical genomics · 2023Article
- Origins of DNA replication in eukaryotes.Molecular cell · 2023Review
- Multiple, short protein binding motifs in ORC1 and CDC6 control the initiation of DNA replication.Molecular cell · 2021Article
- Defining a novel domain that provides an essential contribution to site-specific interaction of Rep protein with DNA.Nucleic acids research · 2021Article
- Article
- Humanizing the yeast origin recognition complex.Nature communications · 2021Article
- Identification andmicroPublication biology · 2021Article
- Review
- Structural insight into the assembly and conformational activation of human origin recognition complex.Cell discovery · 2020Article
- Structural mechanism for replication origin binding and remodeling by a metazoan origin recognition complex and its co-loader Cdc6.Nature communications · 2020Article
- Structural mechanism of helicase loading onto replication origin DNA by ORC-Cdc6.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evolution of metabolic capabilities and molecular features of diplonemids, kinetoplastids, and euglenids.BMC biology · 2020Article
- A new class of disordered elements controls DNA replication through initiator self-assembly.eLife · 2019Article
- 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
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- Rapid Purification and Characterization of Mutant Origin Recognition Complexes in Saccharomyces cerevisiae.Frontiers in microbiology · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, the origin recognition complex (ORC) heterohexamer preferentially binds replication origins to trigger initiation of DNA replication. Crystallographic studies using eubacterial and archaeal ORC orthologs suggested that eukaryotic ORC may bind to origin DNA via putative winged-helix DNA-binding domains and AAA+ ATPase domains. However, the mechanisms how eukaryotic ORC recognizes origin DNA remain elusive. Here, we show in budding yeast that Lys-362 and Arg-367 residues of the largest subunit (Orc1), both outside the aforementioned domains, are crucial for specific binding of ORC to origin DNA. These basic residues, which reside in a putative disordered domain, were dispensable for interaction with ATP and non-specific DNA sequences, suggesting a specific role in recognition. Consistent with this, both residues were required for origin binding of Orc1 in vivo. A truncated Orc1 polypeptide containing these residues solely recognizes ARS sequence with low affinity and Arg-367 residue stimulates sequence specific binding mode of the polypeptide. Lys-362 and Arg-367 residues of Orc1 are highly conserved among eukaryotic ORCs, but not in eubacterial and archaeal orthologs, suggesting a eukaryote-specific mechanism underlying recognition of replication origins by ORC.
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