ArticleNucleic acids research2010
Probing the (H3-H4)2 histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Histone tetrasome dynamics affects chromatin transcription.Nucleic acids research · 2025Article
- In vivo assembly of complete eukaryotic nucleosomes and (H3-H4)-only non-canonical nucleosomal particles in the model bacterium Escherichia coli.Communications biology · 2024Article
- The Oligomerization Landscape of Histones.Biophysical journal · 2019Article
- Hydrogen-Deuterium Exchange Coupled to Top- and Middle-Down Mass Spectrometry Reveals Histone Tail Dynamics before and after Nucleosome Assembly.Structure (London, England : 1993) · 2018Article
- A Molecular Prospective for HIRA Complex Assembly and H3.3-Specific Histone Chaperone Function.Journal of molecular biology · 2017Review
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility.Scientific reports · 2016Article
- The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.Nucleic acids research · 2016Article
- Histones: at the crossroads of peptide and protein chemistry.Chemical reviews · 2015Review
- Chemical and biological tools for the preparation of modified histone proteins.Topics in current chemistry · 2015Article
- The spatial effect of protein deuteration on nitroxide spin-label relaxation: implications for EPR distance measurement.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Histone core modifications regulating nucleosome structure and dynamics.Nature reviews. Molecular cell biology · 2014Review
- Getting down to the core of histone modifications.Chromosoma · 2014Review
- DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues.Nucleic acids research · 2014Article
- Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1.Nature structural & molecular biology · 2013Article
- MtsslWizard: In Silico Spin-Labeling and Generation of Distance Distributions in PyMOL.Applied magnetic resonance · 2012Article
- Global structure of a three-way junction in a phi29 packaging RNA dimer determined using site-directed spin labeling.Journal of the American Chemical Society · 2012Article
- Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.Nature · 2012Article
- NAP1-assisted nucleosome assembly on DNA measured in real time by single-molecule magnetic tweezers.PloS one · 2012Article
- Mechanisms for ATP-dependent chromatin remodelling: the means to the end.The FEBS journal · 2011Review
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Authors and funding
5 authors.
Funding
Abstract
The (H3-H4)(2) histone tetramer forms the central core of nucleosomes and, as such, plays a prominent role in assembly, disassembly and positioning of nucleosomes. Despite its fundamental role in chromatin, the tetramer has received little structural investigation. Here, through the use of pulsed electron-electron double resonance spectroscopy coupled with site-directed spin labelling, we survey the structure of the tetramer in solution. We find that tetramer is structurally more heterogeneous on its own than when sequestered in the octamer or nucleosome. In particular, while the central region including the H3-H3' interface retains a structure similar to that observed in nucleosomes, other regions such as the H3 alphaN helix display increased structural heterogeneity. Flexibility of the H3 alphaN helix in the free tetramer also illustrates the potential for post-translational modifications to alter the structure of this region and mediate interactions with histone chaperones. The approach described here promises to prove a powerful system for investigating the structure of additional assemblies of histones with other important factors in chromatin assembly/fluidity.
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