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

Nucleosome Remodeling02:54

Nucleosome Remodeling

11.3K
Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
11.3K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

14.6K
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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
14.6K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.5K
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...
2.5K
The Nucleosome01:19

The Nucleosome

4.3K
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...
4.3K
The Nucleosome02:33

The Nucleosome

19.1K
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...
19.1K
Chromatin Packaging01:32

Chromatin Packaging

19.8K
Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...
19.8K

You might also read

Related Articles

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

Sort by
Same author

Capturing Structural Heterogeneity in Chromatin Fibers.

Journal of molecular biology·2017
Same author

X-ray structure of the MMTV-A nucleosome core.

Proceedings of the National Academy of Sciences of the United States of America·2016
Same author

Structure of the full-length yeast Arp7-Arp9 heterodimer.

Acta crystallographica. Section D, Biological crystallography·2014
Same author

Nucleosome recognition and spacing by chromatin remodelling factor ISW1a.

Biochemical Society transactions·2012
Same author

Structure and mechanism of the chromatin remodelling factor ISW1a.

Nature·2011
Same author

Robots, pipelines, polyproteins: enabling multiprotein expression in prokaryotic and eukaryotic cells.

Journal of structural biology·2011
Same journal

Biologically Relevant, Cationic Residues in Human Rhinovirus Stabilize Capsid-Bound RNA Duplexes, and Restrict Capsid Flexibility.

Journal of molecular biology·2026
Same journal

Cryo-EM structures of phage T4 infection intermediate.

Journal of molecular biology·2026
Same journal

A classic fold with a twist: Structural architecture of Dhillonvirus phage Bas18.

Journal of molecular biology·2026
Same journal

Tesorai Search: cloud-based database search engine boosts identifications for mass spectrometry proteomics with a pretrained peptide-spectrum deep-learning model.

Journal of molecular biology·2026
Same journal

Characterization of diverse functions of NRF1 nuclear localization sequence.

Journal of molecular biology·2026
Same journal

UPF3A and UPF3B shape the transcriptome cooperatively yet oppose cell function.

Journal of molecular biology·2026
See all related articles

Related Experiment Video

Updated: Feb 19, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.4K

Site-Specific Disulfide Crosslinked Nucleosomes with Enhanced Stability.

Timothy D Frouws1, Philip D Barth1, Timothy J Richmond1

  • 1ETH Zürich, Institute of Molecular Biology and Biophysics, Otto-Stern-Weg 5, 8093 Zürich, Switzerland.

Journal of Molecular Biology
|November 9, 2017
PubMed
Summary
This summary is machine-generated.

Engineered nucleosome core particles (NCPs) with two disulfide crosslinks enhance stability. These stabilized NCPs resist dissociation, aiding biochemical and structural studies.

Keywords:
DNAX-ray crystallographychromatinhexasomehistone

More Related Videos

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.8K
Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

11.6K

Related Experiment Videos

Last Updated: Feb 19, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.4K
Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

10.8K
Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

11.6K

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Nucleosome core particles (NCPs) are fundamental units of DNA packaging.
  • Histone octamer dissociation can complicate structural and biochemical studies of NCPs.
  • Maintaining DNA and histone integrity is crucial for accurate nucleosome research.

Purpose of the Study:

  • To engineer more stable nucleosome core particles (NCPs) for improved experimental handling.
  • To introduce site-specific cysteine crosslinks to enhance NCP structural integrity.
  • To facilitate biochemical and structural investigations through increased NCP stability.

Main Methods:

  • Site-specific cysteine mutations (H2A-N38C, H3-R40C) were introduced into NCPs.
  • Disulfide bonds were formed to crosslink histone proteins and link DNA to the histone octamer.
  • X-ray crystallography was used to determine the structures of engineered NCPs.

Main Results:

  • Two disulfide crosslinks were successfully engineered into NCPs, increasing particle stability.
  • The H2A crosslink stabilizes the histone octamer against dimer dissociation.
  • The H3-DNA crosslink fixes the DNA's translational setting and prevents dilution-driven dissociation.
  • Structural analysis confirmed that crosslinks stabilize NCPs without altering their overall structure.

Conclusions:

  • Engineered crosslinks significantly enhance the stability of nucleosome core particles.
  • These stabilized NCPs exhibit increased resistance to dissociation under various experimental conditions (high dilution, high salt, vitrification).
  • The stabilized NCPs are advantageous for biochemical and structural studies, including cryo-EM and X-ray crystallography.