Evidence map›Paper›PMID 26212454›Full record

ArticleMolecular cell2015

Structural Mechanisms of Nucleosome Recognition by Linker Histones.

Bing-Rui Zhou, Jiansheng Jiang, Hanqiao Feng, Rodolfo Ghirlando, T Sam Xiao, Yawen Bai

Abstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

132 citing papers in PubMed.

  1. Review
  2. Article
  3. Histone Density and Dynamics Shape Mitotic Chromatid Architecture in Xenopus Egg Extracts.Genes to cells : devoted to molecular & cellular mechanisms · 2026
    Article
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  5. Article
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  8. Review
  9. bioRxiv : the preprint server for biology · 2026
    Article
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72 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Bing-Rui ZhouLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Jiansheng JiangLaboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Hanqiao FengLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
T Sam XiaoLaboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Yawen BaiLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: yawen@helix.nih.gov.

Funding

Nucleosome DynamicsZIABC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2009 to 2025
$26.5M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Nucleosome DynamicsZ01BC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2007 to 2008
$329k
Intramural NIH HHS Z01 BC010808NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Linker histones bind to the nucleosome and regulate the structure of chromatin and gene expression. Despite more than three decades of effort, the structural basis of nucleosome recognition by linker histones remains elusive. Here, we report the crystal structure of the globular domain of chicken linker histone H5 in complex with the nucleosome at 3.5 Å resolution, which is validated using nuclear magnetic resonance spectroscopy. The globular domain sits on the dyad of the nucleosome and interacts with both DNA linkers. Our structure integrates results from mutation analyses and previous cross-linking and fluorescence recovery after photobleach experiments, and it helps resolve the long debate on structural mechanisms of nucleosome recognition by linker histones. The on-dyad binding mode of the H5 globular domain is different from the recently reported off-dyad binding mode of Drosophila linker histone H1. We demonstrate that linker histones with different binding modes could fold chromatin to form distinct higher-order structures.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsHistonesModels, MolecularMolecular Sequence DataNucleosomesProtein BindingDrosophila ProteinsHistonesNucleosomes

Identifiers

PMID26212454
PMCPMC4546531

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Registered trials

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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.