ArticleThe EMBO journal2021
Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2A.Z.2.2.
Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- Crystal structure of the histone heterodimer containing histone variant H2A.W.Biochemistry and biophysics reports · 2026Article
- Transport Time Does Not Substantially Alter RNA Expression in Human Ovarian Tissue After Standardized Slow-Freezing for Fertility Preservation.Journal of clinical medicine · 2026Article
- H2B.W2, a spermatocyte-specific histone variant, disrupts nucleosome stability, and reduces chromatin compaction.Nucleic acids research · 2025Article
- Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures.Nature communications · 2025Article
- AlphaFold-guided structural analyses of nucleosome binding proteins.Nucleic acids research · 2025Article
- Structural basis of RNAPII transcription on the nucleosome containing histone variant H2A.B.The EMBO journal · 2025Article
- Multifunctional histone variants in genome function.Nature reviews. Genetics · 2025Review
- Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction.Structure (London, England : 1993) · 2024Article
- Testis-specific H2B.W1 disrupts nucleosome integrity by reducing DNA-histone interactions.Nucleic acids research · 2024Article
- Epigenetic modulation via the C-terminal tail of H2A.Z.Nature communications · 2024Article
- Nucleosomal DNA unwinding pathway through canonical and non-canonical histone disassembly.Communications biology · 2024Article
- The Function of H2A Histone Variants and Their Roles in Diseases.Biomolecules · 2024Review
- Structural and Biochemical Characterization of the Nucleosome Containing Variants H3.3 and H2A.Z.Epigenomes · 2024Article
- H2A.Z is involved in premature aging and DSB repair initiation in muscle fibers.Nucleic acids research · 2024Article
- Roles of Histone H2A Variants in Cancer Development, Prognosis, and Treatment.International journal of molecular sciences · 2024Review
- Structure of native chromatin fibres revealed by Cryo-ET in situ.Nature communications · 2023Article
- Article
- Review
- Correlating histone acetylation with nucleosome core particle dynamics and function.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023Review
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9 authors at 1 institution in 1 country.
Funding
Abstract
Nucleosomes are dynamic entities with wide-ranging compositional variations. Human histone variants H2A.B and H2A.Z.2.2 play critical roles in multiple biological processes by forming unstable nucleosomes and open chromatin structures, but how H2A.B and H2A.Z.2.2 confer these dynamic features to nucleosomes remains unclear. Here, we report cryo-EM structures of nucleosome core particles containing human H2A.B (H2A.B-NCP) at atomic resolution, identifying large-scale structural rearrangements in the histone octamer in H2A.B-NCP. H2A.B-NCP compacts approximately 103 bp of DNA wrapping around the core histones in approximately 1.2 left-handed superhelical turns, in sharp contrast to canonical nucleosome encompassing approximately 1.7 turns of DNA. Micrococcal nuclease digestion assay reveals that nineteen H2A.B-specific residues, including a ROF ("regulating-octamer-folding") sequence of six consecutive residues, are responsible for loosening of H2A.B-NCPs. Unlike H2A.B-NCP, the H2A.Z.2.2-containing nucleosome (Z.2.2-NCP) adopts a less-extended structure and compacts around 125 bp of DNA. Further investigation uncovers a crucial role for the H2A.Z.2.2-specific ROF in both H2A.Z.2.2-NCP opening and SWR1-dependent histone replacement. Taken together, these first high-resolution structure of unstable nucleosomes induced by histone H2A variants elucidate specific functions of H2A.B and H2A.Z.2.2 in enhancing chromatin dynamics.
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