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- W4313255008 endingPage "111858" @default.
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- W4313255008 abstract "The histone chaperone FACT (facilitates chromatin transcription) enhances transcription in eukaryotic cells, targeting DNA-protein interactions. FACT, a heterodimer in humans, comprises SPT16 and SSRP1 subunits. We measure nucleosome stability and dynamics in the presence of FACT and critical component domains. Optical tweezers quantify FACT/subdomain binding to nucleosomes, displacing the outer wrap of DNA, disrupting direct DNA-histone (core site) interactions, altering the energy landscape of unwrapping, and increasing the kinetics of DNA-histone disruption. Atomic force microscopy reveals nucleosome remodeling, while single-molecule fluorescence quantifies kinetics of histone loss for disrupted nucleosomes, a process accelerated by FACT. Furthermore, two isolated domains exhibit contradictory functions; while the SSRP1 HMGB domain displaces DNA, SPT16 MD/CTD stabilizes DNA-H2A/H2B dimer interactions. However, only intact FACT tethers disrupted DNA to the histones and supports rapid nucleosome reformation over several cycles of force disruption/release. These results demonstrate that key FACT domains combine to catalyze both nucleosome disassembly and reassembly." @default.
- W4313255008 created "2023-01-06" @default.
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- W4313255008 date "2022-12-01" @default.
- W4313255008 modified "2023-10-14" @default.
- W4313255008 title "Human FACT subunits coordinate to catalyze both disassembly and reassembly of nucleosomes" @default.
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- W4313255008 doi "https://doi.org/10.1016/j.celrep.2022.111858" @default.
- W4313255008 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36577379" @default.
- W4313255008 hasPublicationYear "2022" @default.
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