ArticleProceedings of the National Academy of Sciences of the United States of America2020
Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 17 citations in OpenAlex.
- Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme.Science advances · 2026Article
- Structural and functional insights into the nuclear role of Parkinson's disease-associated α-synuclein as a histone chaperone.Communications biology · 2025Article
- Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex.Molecular cell · 2024Article
- Dual engagement of the nucleosomal acidic patches is essential for deposition of histone H2A.Z by SWR1C.eLife · 2024Article
- Structural insights into histone exchange by human SRCAP complex.Cell discovery · 2024Article
- Multivalency of nucleosome recognition by LEDGF.Nucleic acids research · 2023Article
- Epstein-Barr virus protein BKRF4 restricts nucleosome assembly to suppress host antiviral responses.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Coordinated DNA and histone dynamics drive accurate histone H2A.Z exchange.Science advances · 2022Article
- Collaboration through chromatin: motors of transcription and chromatin structure.Journal of molecular biology · 2021Review
- Thermodynamic and sequential characteristics of phase separation and droplet formation for an intrinsically disordered region/protein ensemble.PLoS computational biology · 2021Article
- DJ-1 Proteoforms in Breast Cancer Cells: The Escape of Metabolic Epigenetic Misregulation.Cells · 2020Article
- Overcoming off-targets: assessing Western blot signals for Bcnt/Cfdp1, a tentative component of the chromatin remodeling complex.Bioscience reports · 2020Article
- Structure of a single-chain H2A/H2B dimer.Acta crystallographica. Section F, Structural biology communications · 2020Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The SWR complex edits the histone composition of nucleosomes at promoters to facilitate transcription by replacing the two nucleosomal H2A-H2B (A-B) dimers with H2A.Z-H2B (Z-B) dimers. Swc5, a subunit of SWR, binds to A-B dimers, but its role in the histone replacement reaction was unclear. In this study, we showed that Swc5 uses a tandem DEF/Y motif within an intrinsically disordered region to engage the A-B dimer. A 2.37-Å X-ray crystal structure of the histone binding domain of Swc5 in complex with an A-B dimer showed that consecutive acidic residues and flanking hydrophobic residues of Swc5 form a cap over the histones, excluding histone-DNA interaction. Mutations in Swc5 DEF/Y inhibited the nucleosome editing function of SWR in vitro. Swc5 DEF/Y interacts with histones in vivo, and the extent of this interaction is dependent on the remodeling ATPase of SWR, supporting a model in which Swc5 acts as a wedge to promote A-B dimer eviction. Given that DEF/Y motifs are found in other evolutionary unrelated chromatin regulators, this work provides the molecular basis for a general strategy used repeatedly during eukaryotic evolution to mobilize histones in various genomic functions.
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