ArticleiScience2020
Partial Replacement of Nucleosomal DNA with Human FACT Induces Dynamic Exposure and Acetylation of Histone H3 N-Terminal Tails.
Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 17 citations in OpenAlex.
- Kaiso reads methylated CpGs at nucleosome entry/exit and displaces the H3 tail.bioRxiv : the preprint server for biology · 2026Article
- Differential histone tail citrullination by PAD Enzymes observed via NMR spectroscopy.bioRxiv : the preprint server for biology · 2026Article
- Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation and alters its dynamics.Communications biology · 2026Article
- G34R cancer mutation alters the conformational ensemble and dynamics of the histone H3.3 tails.Nucleic acids research · 2026Article
- Dynamic networks of intrinsically disordered regions in nuclear proteins.Biophysics and physicobiology · 2026Article
- Arginine anchor points govern H3 tail dynamics.Frontiers in molecular biosciences · 2023Article
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- FACT modulates the conformations of histone H2A and H2B N-terminal tails within nucleosomes.Communications biology · 2022Article
- Visualizing Conformational Ensembles of the Nucleosome by NMR.ACS chemical biology · 2022Review
- Characteristic H3 N-tail dynamics in the nucleosome core particle, nucleosome, and chromatosome.iScience · 2022Article
- Nucleosome composition regulates the histone H3 tail conformational ensemble and accessibility.Nucleic acids research · 2021Article
- Drugging the "Undruggable" MYCN Oncogenic Transcription Factor: Overcoming Previous Obstacles to Impact Childhood Cancers.Cancer research · 2021Review
- Characterization of functional disordered regions within chromatin-associated proteins.iScience · 2021Review
- Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The FACT (facilitates chromatin transcription) complex, comprising SPT16 and SSRP1, conducts structural alterations during nucleosome unwrapping. Our previous cryoelectron microscopic (cryo-EM) analysis revealed the first intermediate structure of an unwrapped nucleosome with human FACT, in which 112-bp DNA and the phosphorylated intrinsically disordered (pAID) segment of SPT16 jointly wrapped around the histone core instead of 145-bp DNA. Using NMR, here we clarified that the histone H3 N-terminal tails, unobserved in the cryo-EM structure, adopt two different conformations reflecting their asymmetric locations at entry/exit sites: one corresponds to the original nucleosome site buried in two DNA gyres (DNA side), whereas the other, comprising pAID and DNA, is more exposed to the solvent (pAID side). NMR real-time monitoring showed that H3 acetylation is faster on the pAID side than on the DNA side. Our findings highlight that accessible conformations of H3 tails are created by the replacement of nucleosomal DNA with pAID.
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