ArticleJournal of molecular biology2016
A Small Number of Residues Can Determine if Linker Histones Are Bound On or Off Dyad in the Chromatosome.
Article in Journal of molecular biology, 2016. 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.
- Linker Histones: The Multiple Binding Modes of the Enigmatic 5th Histone.Biomolecules · 2026Review
- Contributions of Local Structural and Energetic Features of DNA to Large-scale Genomic Organization.Journal of molecular biology · 2026Review
- Linker histone H1.5 contributes to centromere integrity.Nucleic acids research · 2026Article
- A DNA condensation code for linker histones.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Regulation of chromatin architecture by protein binding: insights from molecular modeling.Biophysical reviews · 2024Review
- Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy.Journal of the American Chemical Society · 2023Article
- Epigallocatechin Gallate Affects the Structure of Chromatosomes, Nucleosomes and Their Complexes with PARP1.International journal of molecular sciences · 2023Article
- Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023Review
- The Role of PARP1 and PAR in ATP-Independent Nucleosome Reorganisation during the DNA Damage Response.Genes · 2022Review
- Article
- Molecular organization of the early stages of nucleosome phase separation visualized by cryo-electron tomography.Molecular cell · 2022Article
- H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes.Biochemistry · 2022Article
- Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges.Protein science : a publication of the Protein Society · 2022Article
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- DNA sequence-dependent positioning of the linker histone in a nucleosome: A single-pair FRET study.Biophysical journal · 2021Article
- Article
- A glitch in the snitch: the role of linker histone H1 in shaping the epigenome in normal and diseased cells.Open biology · 2021Review
- The Dynamic Influence of Linker Histone Saturation within the Poly-Nucleosome Array.Journal of molecular biology · 2021Article
- Integrating single-molecule FRET and biomolecular simulations to study diverse interactions between nucleic acids and proteins.Essays in biochemistry · 2021Review
- Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.Journal of molecular biology · 2021Article
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6 authors.
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Abstract
Linker histones bind to the nucleosome and regulate the structure and function of chromatin. We have previously shown that the globular domains of chicken H5 and Drosophila H1 linker histones bind to the nucleosome with on- or off-dyad modes, respectively. To explore the determinant for the distinct binding modes, we investigated the binding of a mutant globular domain of H5 to the nucleosome. This mutant, termed GH5_pMut, includes substitutions of five globular domain residues of H5 with the corresponding residues in the globular domain of Drosophila H1. The residues at these five positions play important roles in nucleosome binding by either H5 or Drosophila H1. NMR and spin-labeling experiments showed that GH5_pMut bound to the nucleosome off the dyad. We further found that the nucleosome array condensed by either the GH5_pMut or the globular domain of Drosophila H1 displayed a similar sedimentation coefficient, whereas the same nucleosome array condensed by the wild-type globular domain of H5 showed a much larger sedimentation coefficient. Moreover, NMR and spin-labeling results from the study of the nucleosome in complex with the full-length human linker histone H1.0, whose globular domain shares high sequence conservation with the corresponding globular domain of H5, are consistent with an on-dyad binding mode. Taken together, our results suggest that a small number of residues in the globular domain of a linker histone can control its binding location on the nucleosome and higher-order chromatin structure.
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