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Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.9K
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Heterochromatin02:38

Heterochromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
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Heterochromatin02:38

Heterochromatin

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The Nucleosome01:19

The Nucleosome

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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
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The Nucleosome02:33

The Nucleosome

18.3K
DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
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Histone Modification02:32

Histone Modification

15.9K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Related Experiment Video

Updated: Jan 13, 2026

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
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Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

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Linker histone H1.5 contributes to centromere integrity.

Ankita Saha1,2, Minh Bui1, Daniël P Melters1

  • 1National Cancer Institute, Centre for Cancer Research, Laboratory Receptor Biology and Gene Expression, Bethesda, MD 20892, United States.

Nucleic Acids Research
|January 12, 2026
PubMed
Summary
This summary is machine-generated.

Specific histone H1 variants, like H1.5, interact with centromeric chromatin and CENP-A. Depleting H1.5 disrupts centromeric transcription, CENP-A loading, and causes mitotic defects, revealing a role in mitotic integrity.

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Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A
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Expression Analysis of Mammalian Linker-histone Subtypes
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Expression Analysis of Mammalian Linker-histone Subtypes

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Related Experiment Videos

Last Updated: Jan 13, 2026

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
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Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

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Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A
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Expression Analysis of Mammalian Linker-histone Subtypes
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Expression Analysis of Mammalian Linker-histone Subtypes

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Area of Science:

  • Cell biology
  • Epigenetics
  • Molecular genetics

Background:

  • Mammalian H1 linker histones are crucial for chromatin modulation.
  • H1 variants have specific genomic distributions influencing gene expression and chromatin architecture.
  • Previous studies provided conflicting evidence regarding H1 histone presence at centromeres.

Purpose of the Study:

  • To investigate the impact of H1 histones on centromeric chromatin.
  • To determine if H1 variants physically interact with centromeric components.

Main Methods:

  • In vitro assays to test interactions between H1 variants and CENP-A mononucleosomes.
  • In vivo studies using human cells to assess H1.5 localization at centromeres.
  • Chromatin immunoprecipitation (ChIP) to confirm H1.5 interaction with centromeric chromatin.
  • Targeted depletion of H1.5 to observe downstream effects.

Main Results:

  • Three H1 linker histone variants, including H1.5, physically interact with CENP-A mononucleosomes in vitro.
  • H1.5 localizes to centromeres in human cells.
  • Depletion of H1.5 led to loss of centromeric α-satellite transcription.
  • H1.5 depletion reduced new CENP-A loading and altered kinetochore protein gene expression.
  • Mitotic defects were observed upon H1.5 depletion.

Conclusions:

  • Specific H1 histone variants, particularly H1.5, interact with centromeric chromatin and CENP-A.
  • H1.5 plays a significant role in maintaining centromeric integrity and function.
  • These findings suggest a novel role for H1.5 in regulating mitotic integrity.