Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.5K
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...
4.5K
Heterochromatin02:38

Heterochromatin

14.6K
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...
14.6K
The Nucleosome01:19

The Nucleosome

2.6K
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...
2.6K
Histone Modification02:32

Histone Modification

14.1K
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...
14.1K
Chromosome Structure02:40

Chromosome Structure

23.7K
A functional eukaryotic chromosome must contain three elements: a centromere, telomeres, and numerous origins of replication.
The centromere is a DNA sequence that links sister chromatids. This is also where kinetochores, protein complexes to which spindle microtubules attach, are constructed after the chromosome is replicated. The kinetochores allow the spindle microtubules to move the chromosomes within the cell during cell division.
Telomeres consist of non-coding repetitive nucleotide...
23.7K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

1.3K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
1.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Rethinking how research is reviewed and published.

eLife·2026
Same author

ReMeDy: A Flexible Statistical Framework For Region-based Detection of DNA Methylation Dysregulation.

bioRxiv : the preprint server for biology·2026
Same author

Single amino-acid differences define H2B variants and modify chromatin accessibility to induce EMT in breast cancer.

Oncogene·2026
Same author

Linker histone H1.5 contributes to centromere integrity.

Nucleic acids research·2026
Same author

MetaChrome: An Open-Source, User-Friendly Tool for Automated Metaphase Chromosome Analysis.

bioRxiv : the preprint server for biology·2025
Same author

Oncogenic lncRNA transgene transcription modulates epigenetic memory at a naïve chromosomal locus.

Nucleus (Austin, Tex.)·2025

Related Experiment Video

Updated: Sep 18, 2025

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
05:35

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

Published on: March 3, 2016

15.3K

Linker Histone H1.5 Contributes to Centromere Integrity in Human Cells.

Ankita Saha1, Minh Bui1, Daniël P Melters1

  • 1National Cancer Institute, Centre for Cancer Research, Laboratory Receptor Biology and Gene Expression, Bethesda, Maryland, USA.

Biorxiv : the Preprint Server for Biology
|June 26, 2025
PubMed
Summary
This summary is machine-generated.

Histone H1.5 binds centromeric protein A (CENP-A) nucleosomes, impacting centromeric transcription and mitotic integrity. This study reveals a novel role for histone H1 in regulating cell division.

More Related Videos

Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A
09:02

Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A

Published on: June 10, 2020

5.7K
Expression Analysis of Mammalian Linker-histone Subtypes
14:40

Expression Analysis of Mammalian Linker-histone Subtypes

Published on: March 19, 2012

13.9K

Related Experiment Videos

Last Updated: Sep 18, 2025

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
05:35

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

Published on: March 3, 2016

15.3K
Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A
09:02

Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A

Published on: June 10, 2020

5.7K
Expression Analysis of Mammalian Linker-histone Subtypes
14:40

Expression Analysis of Mammalian Linker-histone Subtypes

Published on: March 19, 2012

13.9K

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cell Biology

Background:

  • Mammalian linker histones (H1 variants) modulate chromatin structure and gene expression.
  • The precise role of H1 histones at centromeres remains controversial.
  • Centromeric chromatin is crucial for chromosome segregation during cell division.

Purpose of the Study:

  • To investigate the interaction of H1 histone variants with centromeric chromatin.
  • To determine the functional significance of H1.5 at the centromere.
  • To elucidate the role of H1 histones in maintaining mitotic integrity.

Main Methods:

  • In vitro binding assays using purified proteins.
  • Chromatin immunoprecipitation in human cells.
  • RNA sequencing to assess centromeric transcription.
  • Analysis of mitotic defects and CENP-A loading.

Main Results:

  • Histone H1.5 directly interacts with CENP-A nucleosomes in vitro.
  • H1.0 and H1.2 also bind CENP-A nucleosomes with varying affinities.
  • H1.5 localizes to centromeres in human cells and interacts with CENP-A nucleosomes.
  • H1.5 depletion disrupts centromeric transcription, reduces CENP-A loading, and causes mitotic defects.

Conclusions:

  • Histone H1.5 plays a critical role in centromeric chromatin regulation.
  • H1 histone variants can interact with CENP-A nucleosomes, suggesting broader roles.
  • Histone H1 is essential for maintaining mitotic integrity in human cells.