ArticleCancers2017
Stabilization of Nucleosomes by Histone Tails and by FACT Revealed by spFRET Microscopy.
Article in Cancers, 2017. 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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Who cites it
23 citing papers in PubMed, 42 citations in OpenAlex.
- Insights into FACT in Cancers with Targeted Therapeutic Implications.Molecular and cellular biology · 2026Review
- An intrinsically disordered region of Ubp10 regulates its binding and activity on ubiquitinated histone substrates.Protein science : a publication of the Protein Society · 2025Article
- Transcriptional regulation of FACT involves Coordination of chromatin accessibility and CTCF binding.The Journal of biological chemistry · 2024Article
- Interactions of Nucleosomes with Acidic Patch-Binding Peptides: A Combined Structural Bioinformatics, Molecular Modeling, Fluorescence Polarization, and Single-Molecule FRET Study.International journal of molecular sciences · 2023Article
- Structure and Dynamics of Compact Dinucleosomes: Analysis by Electron Microscopy and spFRET.International journal of molecular sciences · 2023Article
- Review
- Opposing Roles of FACT for Euchromatin and Heterochromatin in Yeast.Biomolecules · 2023Review
- Studying Chromatin Epigenetics with Fluorescence Microscopy.International journal of molecular sciences · 2022Review
- Mechanism of curaxin-dependent nucleosome unfolding by FACT.Frontiers in molecular biosciences · 2022Article
- Binding of regulatory proteins to nucleosomes is modulated by dynamic histone tails.Nature communications · 2021Article
- APE1 and SSRP1 is overexpressed in muscle invasive bladder cancer and associated with poor survival.Heliyon · 2021Article
- The role of FACT in managing chromatin: disruption, assembly, or repair?Nucleic acids research · 2020Review
- Partial Replacement of Nucleosomal DNA with Human FACT Induces Dynamic Exposure and Acetylation of Histone H3 N-Terminal Tails.iScience · 2020Article
- Structural visualization of key steps in nucleosome reorganization by human FACT.Scientific reports · 2019Article
- The anti-cancer drugs curaxins target spatial genome organization.Nature communications · 2019Article
- Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function.Journal of cancer metastasis and treatment · 2019Article
- Transcription Promotes the Interaction of the FAcilitates Chromatin Transactions (FACT) Complex with Nucleosomes inGenetics · 2018Article
- Mechanism of FACT removal from transcribed genes by anticancer drugs curaxins.Science advances · 2018Article
- Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- Functional roles of the DNA-binding HMGB domain in the histone chaperone FACT in nucleosome reorganization.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
A correct chromatin structure is important for cell viability and is tightly regulated by numerous factors. Human protein complex FACT (facilitates chromatin transcription) is an essential factor involved in chromatin transcription and cancer development. Here FACT-dependent changes in the structure of single nucleosomes were studied with single-particle Förster resonance energy transfer (spFRET) microscopy using nucleosomes labeled with a donor-acceptor pair of fluorophores, which were attached to the adjacent gyres of DNA near the contact between H2A-H2B dimers. Human FACT and its version without the C-terminal domain (CTD) and the high mobility group (HMG) domain of the structure-specific recognition protein 1 (SSRP1) subunit did not change the structure of the nucleosomes, while FACT without the acidic C-terminal domains of the suppressor of Ty 16 (Spt16) and the SSRP1 subunits caused nucleosome aggregation. Proteolytic removal of histone tails significantly disturbed the nucleosome structure, inducing partial unwrapping of nucleosomal DNA. Human FACT reduced DNA unwrapping and stabilized the structure of tailless nucleosomes. CTD and/or HMG domains of SSRP1 are required for this FACT activity. In contrast, previously it has been shown that yeast FACT unfolds (reorganizes) nucleosomes using the CTD domain of SSRP1-like Pol I-binding protein 3 subunit (Pob3). Thus, yeast and human FACT complexes likely utilize the same domains for nucleosome reorganization and stabilization, respectively, and these processes are mechanistically similar.
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Registered trials
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