ArticleMolecular and cellular biology2011
Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 69 citations in OpenAlex.
- Linker Histones: The Multiple Binding Modes of the Enigmatic 5th Histone.Biomolecules · 2026Review
- Conformations of Linker Histone H1 Bound to Nucleosome Arrays.Journal of molecular biology · 2026Article
- Linker histones consolidate heterogenous nucleosome fiber contacts by linking together multiple nucleosomes.Nature communications · 2026Article
- Altering metabolism programs cell identity via NADThe EMBO journal · 2025Article
- Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes.Journal of molecular biology · 2023Article
- H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes.Biochemistry · 2022Article
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- A glitch in the snitch: the role of linker histone H1 in shaping the epigenome in normal and diseased cells.Open biology · 2021Review
- Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain.Nucleic acids research · 2020Article
- Emergence of chromatin hierarchical loops from protein disorder and nucleosome asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Robust Method for the Purification and Characterization of Recombinant Human Histone H1 Variants.Biochemistry · 2019Article
- A nucleosome-free region locally abrogates histone H1-dependent restriction of linker DNA accessibility in chromatin.The Journal of biological chemistry · 2018Article
- A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.Journal of biomolecular NMR · 2018Article
- The interplay between H2A.Z and H3K9 methylation in regulating HP1α binding to linker histone-containing chromatin.Nucleic acids research · 2018Article
- MacroH2A histone variants limit chromatin plasticity through two distinct mechanisms.EMBO reports · 2018Article
- H1.0 Linker Histone as an Epigenetic Regulator of Cell Proliferation and Differentiation.Genes · 2018Review
- HMGN1 and 2 remodel core and linker histone tail domains within chromatin.Nucleic acids research · 2017Article
- Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1.Molecular cell · 2017Article
- Linker histones: novel insights into structure-specific recognition of the nucleosome.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2017Review
- Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Chromosoma · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Linker histones play essential roles in the chromatin structure of higher eukaryotes. While binding to the surface of nucleosomes is directed by an ∼ 80-amino-acid-residue globular domain, the structure and interactions of the lysine-rich ∼ 100-residue C-terminal domain (CTD), primarily responsible for the chromatin-condensing functions of linker histones, are poorly understood. By quantitatively analyzing binding of a set of H1 CTD deletion mutants to nucleosomes containing various lengths of linker DNA, we have identified interactions between distinct regions of the CTD and nucleosome linker DNA at least 21 bp from the edge of the nucleosome core. Importantly, partial CTD truncations caused increases in H1 binding affinity, suggesting that significant entropic costs are incurred upon binding due to CTD folding. van't Hoff entropy/enthalpy analysis and intramolecular fluorescent resonance energy transfer (FRET) studies indicate that the CTD undergoes substantial nucleosome-directed folding, in a manner that is distinct from that which occurs upon H1 binding to naked DNA. In addition to defining critical interactions between the H1 CTD and linker DNA, our data indicate that the H1 CTD is an intrinsically disordered domain and provide important insights into the biological function of this protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.