ArticleScientific reports2016
Solution structure of the isolated histone H2A-H2B heterodimer.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 34 citations in OpenAlex.
- Crystal structure of the histone heterodimer containing histone variant H2A.W.Biochemistry and biophysics reports · 2026Article
- Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026Article
- Dynamic networks of intrinsically disordered regions in nuclear proteins.Biophysics and physicobiology · 2026Article
- The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain.Molecular cell · 2025Article
- Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA mimicry and histone chaperone efficiency.iScience · 2024Article
- A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription.Oncogenesis · 2024Article
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Article
- Characteristic H3 N-tail dynamics in the nucleosome core particle, nucleosome, and chromatosome.iScience · 2022Article
- Biophysics is reshaping our perception of the epigenome: from DNA-level to high-throughput studies.Biophysical reports · 2021Review
- Mapping the electrostatic potential of the nucleosome acidic patch.Scientific reports · 2021Article
- Structural Heterogeneity of Human Histone H2A.1.The journal of physical chemistry. B · 2021Article
- COMMD4 functions with the histone H2A-H2B dimer for the timely repair of DNA double-strand breaks.Communications biology · 2021Article
- Structure of a single-chain H2A/H2B dimer.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structural visualization of key steps in nucleosome reorganization by human FACT.Scientific reports · 2019Article
- Histone Tail Dynamics in Partially Disassembled Nucleosomes During Chromatin Remodeling.Frontiers in molecular biosciences · 2019Article
- Replication-dependent histone isoforms: a new source of complexity in chromatin structure and function.Nucleic acids research · 2018Review
- DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface.Nucleic acids research · 2018Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During chromatin-regulated processes, the histone H2A-H2B heterodimer functions dynamically in and out of the nucleosome. Although detailed crystal structures of nucleosomes have been established, that of the isolated full-length H2A-H2B heterodimer has remained elusive. Here, we have determined the solution structure of human H2A-H2B by NMR coupled with CS-Rosetta. H2A and H2B each contain a histone fold, comprising four α-helices and two β-strands (α1-β1-α2-β2-α3-αC), together with the long disordered N- and C-terminal H2A tails and the long N-terminal H2B tail. The N-terminal αN helix, C-terminal β3 strand, and 310 helix of H2A observed in the H2A-H2B nucleosome structure are disordered in isolated H2A-H2B. In addition, the H2A α1 and H2B αC helices are not well fixed in the heterodimer, and the H2A and H2B tails are not completely random coils. Comparison of hydrogen-deuterium exchange, fast hydrogen exchange, and {(1)H}-(15)N hetero-nuclear NOE data with the CS-Rosetta structure indicates that there is some conformation in the H2A 310 helical and H2B Lys11 regions, while the repression domain of H2B (residues 27-34) exhibits an extended string-like structure. This first structure of the isolated H2A-H2B heterodimer provides insight into its dynamic functions in chromatin.
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