ArticleThe EMBO journal2006
Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- MacroH2A-Mediated Gene Repression through Nucleosome Compaction and Remodeling Inhibition.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of RNAPII transcription on the nucleosome containing histone variant H2A.B.The EMBO journal · 2025Article
- 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
- Histone H2A variant H2A.B is enriched in transcriptionally active and replicating HSV-1 lytic chromatin.Journal of virology · 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
- Casting histone variants during mammalian reproduction.Chromosoma · 2023Review
- Unusual nucleosome formation and transcriptome influence by the histone H3mm18 variant.Nucleic acids research · 2022Article
- H2A.B is a cancer/testis factor involved in the activation of ribosome biogenesis in Hodgkin lymphoma.EMBO reports · 2021Article
- Effects of H2A.B incorporation on nucleosome structures and dynamics.Biophysical journal · 2021Article
- The dark side of histones: genomic organization and role of oncohistones in cancer.Clinical epigenetics · 2021Review
- Histone variants at a glance.Journal of cell science · 2021Review
- Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome.Communications biology · 2021Article
- Short H2A histone variants are expressed in cancer.Nature communications · 2021Article
- Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2A.Z.2.2.The EMBO journal · 2021Article
- Biparental contributions of the H2A.B histone variant control embryonic development in mice.PLoS biology · 2020Article
- Review
- The N-terminal and C-terminal halves of histone H2A.Z independently function in nucleosome positioning and stability.Genes to cells : devoted to molecular & cellular mechanisms · 2020Article
- Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures.Epigenetics & chromatin · 2020Article
- Review
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The histone variant H2A.Bbd appeared to be associated with active chromatin, but how it functions is unknown. We have dissected the properties of nucleosome containing H2A.Bbd. Atomic force microscopy (AFM) and electron cryo-microscopy (cryo-EM) showed that the H2A.Bbd histone octamer organizes only approximately 130 bp of DNA, suggesting that 10 bp of each end of nucleosomal DNA are released from the octamer. In agreement with this, the entry/exit angle of the nucleosomal DNA ends formed an angle close to 180 degrees and the physico-chemical analysis pointed to a lower stability of the variant particle. Reconstitution of nucleosomes with swapped-tail mutants demonstrated that the N-terminus of H2A.Bbd has no impact on the nucleosome properties. AFM, cryo-EM and chromatin remodeling experiments showed that the overall structure and stability of the particle, but not its property to interfere with the SWI/SNF induced remodeling, were determined to a considerable extent by the H2A.Bbd docking domain. These data show that the whole H2A.Bbd histone fold domain is responsible for the unusual properties of the H2A.Bbd nucleosome.
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