ArticleNucleic acids research2011
The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 66 citations in OpenAlex.
- DNA Sequence and Histone Variant H2A.Z Jointly Govern Nucleosome Unwrapping Pathways.bioRxiv : the preprint server for biology · 2026Article
- Crystal structure of the histone heterodimer containing histone variant H2A.W.Biochemistry and biophysics reports · 2026Article
- Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif.Genes & development · 2025Article
- Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif.bioRxiv : the preprint server for biology · 2025Article
- VprBP regulates osteoclast differentiation via an epigenetic mechanism involving histone H2A phosphorylation.Epigenetics & chromatin · 2024Article
- Molecular Dynamics Simulations of Nucleosomes Containing Histone Variant H2A.J.International journal of molecular sciences · 2024Article
- Nucleosomal DNA unwinding pathway through canonical and non-canonical histone disassembly.Communications biology · 2024Article
- Identification of a novel DNA oxidative damage repair pathway, requiring the ubiquitination of the histone variant macroH2A1.1.BMC biology · 2024Article
- VprBP/DCAF1 Triggers Melanomagenic Gene Silencing through Histone H2A Phosphorylation.Biomedicines · 2023Article
- Correlating histone acetylation with nucleosome core particle dynamics and function.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure of the human inner kinetochore CCAN complex and its significance for human centromere organization.Molecular cell · 2022Article
- Unusual nucleosome formation and transcriptome influence by the histone H3mm18 variant.Nucleic acids research · 2022Article
- Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome.Communications biology · 2021Article
- Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2A.Z.2.2.The EMBO journal · 2021Article
- Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures.Epigenetics & chromatin · 2020Article
- Phase-plate cryo-EM structure of the Widom 601 CENP-A nucleosome core particle reveals differential flexibility of the DNA ends.Nucleic acids research · 2020Article
- Elucidating the influence of linker histone variants on chromatosome dynamics and energetics.Nucleic acids research · 2020Article
- Review
- Modelling and DNA topology of compact 2-start and 1-start chromatin fibres.Nucleic acids research · 2019Article
- Generation of Remosomes by the SWI/SNF Chromatin Remodeler Family.Scientific reports · 2019Article
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12 authors at 7 institutions in 1 country.
Funding
Abstract
Histone variants within the H2A family show high divergences in their C-terminal regions. In this work, we have studied how these divergences and in particular, how a part of the H2A COOH-terminus, the docking domain, is implicated in both structural and functional properties of the nucleosome. Using biochemical methods in combination with Atomic Force Microscopy and Electron Cryo-Microscopy, we show that the H2A-docking domain is a key structural feature within the nucleosome. Deletion of this domain or replacement with the incomplete docking domain from the variant H2A.Bbd results in significant structural alterations in the nucleosome, including an increase in overall accessibility to nucleases, un-wrapping of ∼10 bp of DNA from each end of the nucleosome and associated changes in the entry/exit angle of DNA ends. These structural alterations are associated with a reduced ability of the chromatin remodeler RSC to both remodel and mobilize the nucleosomes. Linker histone H1 binding is also abrogated in nucleosomes containing the incomplete docking domain of H2A.Bbd. Our data illustrate the unique role of the H2A-docking domain in coordinating the structural-functional aspects of the nucleosome properties. Moreover, our data suggest that incorporation of a 'defective' docking domain may be a primary structural role of H2A.Bbd in chromatin.
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