ArticleFrontiers in molecular biosciences2022
Mechanism of curaxin-dependent nucleosome unfolding by FACT.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- The basic domain of Suv39h2 buffers mitoxantrone-induced heterochromatin destabilization.iScience · 2026Article
- Mammalian innate antiviral defenses: beyond interferon.Journal of virology · 2025Review
- Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025Review
- Abo1 ATPase facilitates the dissociation of FACT from chromatin.Nucleic acids research · 2025Article
- Anticancer Plant Secondary Metabolites Induce Linker Histone Depletion from Chromatin.Frontiers in bioscience (Landmark edition) · 2024Article
- Comparative Review on Cancer Pathology from Aberrant Histone Chaperone Activity.International journal of molecular sciences · 2024Review
- Insights into the Mechanism of Curaxin CBL0137 Epigenetic Activity: The Induction of DNA Demethylation and the Suppression of BET Family Proteins.International journal of molecular sciences · 2023Article
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
Human FACT (FACT) is a multifunctional histone chaperone involved in transcription, replication and DNA repair. Curaxins are anticancer compounds that induce FACT-dependent nucleosome unfolding and trapping of FACT in the chromatin of cancer cells (c-trapping) through an unknown molecular mechanism. Here, we analyzed the effects of curaxin CBL0137 on nucleosome unfolding by FACT using spFRET and electron microscopy. By itself, FACT adopted multiple conformations, including a novel, compact, four-domain state in which the previously unresolved NTD of the SPT16 subunit of FACT was localized, apparently stabilizing a compact configuration. Multiple, primarily open conformations of FACT-nucleosome complexes were observed during curaxin-supported nucleosome unfolding. The obtained models of intermediates suggest "decision points" in the unfolding/folding pathway where FACT can either promote disassembly or assembly of nucleosomes, with the outcome possibly being influenced by additional factors. The data suggest novel mechanisms of nucleosome unfolding by FACT and c-trapping by curaxins.
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