ArticleMolecular biology reports2010
Human initiation protein Orc4 prefers triple stranded DNA.
Article in Molecular biology reports, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Three- and four-stranded nucleic acid structures and their ligands.RSC chemical biology · 2025Review
- Chemoproteomic profiling unveils binding and functional diversity of endogenous proteins that interact with endogenous triplex DNA.Nature chemistry · 2024Article
- Deletion of Orc4 during oogenesis severely reduces polar body extrusion and blocks zygotic DNA replication†.Biology of reproduction · 2022Article
- Higher Order Oligomerization of the Licensing ORC4 Protein Is Required for Polar Body Extrusion in Murine Meiosis.Journal of cellular biochemistry · 2017Article
- Article
- p53 Specifically Binds Triplex DNA In Vitro and in Cells.PloS one · 2016Article
- DNA-protein interaction dynamics at the Lamin B2 replication origin.Cell cycle (Georgetown, Tex.) · 2015Article
- Human origin recognition complex binds preferentially to G-quadruplex-preferable RNA and single-stranded DNA.The Journal of biological chemistry · 2013Article
- Triple helix-interacting proteins and cancer.OA molecular oncology · 2013Article
- Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In higher eukaryotes mechanism of DNA replication origin recognition and binding by origin recognition complex (ORC) is still unknown. Origin transfer studies have shown that origin sites are genetically determined, containing functionally interchangeable modules. One of such modules from the human lamin B2 origin of replication has the ability to adopt unorthodox structure partly composed of intramolecular triplex. Sequences involved in triplex formation coincide with ORC binding sites both in vitro and in vivo. To explore potential significance of unorthodox DNA structures in origin recognition by ORC, we tested DNA binding properties of human ORC subunit 4 (HsOrc4) which has independent DNA binding activity in vitro and similar binding characteristics as ORC holocomplex. Our results demonstrated that DNA binding activity of HsOrc4 depends on length and structure of DNA with triplex being the protein's preferred binding target. Such feature could play part in origin selection through directing ORC to DNA sequence prone to adopt unorthodox structure.
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Registered trials
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