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

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...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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...
The Nucleosome01:19

The Nucleosome

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...
The Nucleosome02:33

The Nucleosome

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...
The Nucleosome02:33

The Nucleosome

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...

You might also read

Related Articles

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

Sort by
Same author

Structure of the human HIRA histone chaperone with a nucleosome suggests a stepwise nucleosome assembly mechanism.

bioRxiv : the preprint server for biology·2026
Same author

TFAM organizes DNA into compact higher order structures.

bioRxiv : the preprint server for biology·2026
Same author

Histone diversity in the archaeal domain of life.

Nature communications·2026
Same author

Fluorine-Thiol Displacement Stapling on the Disordered α<sub>B</sub> of pKID Domain Increases Its Helicity and Affinity to KIX.

Synlett : accounts and rapid communications in synthetic organic chemistry·2026
Same author

The Expanding Histone Universe: Histone-Based DNA Organization in Noneukaryotic Organisms.

Annual review of biophysics·2025
Same author

Histone PARylation factor 1: a review of its role in the DNA damage response.

Nucleic acids research·2025
Same journal

Correction to 'New origin firing is inhibited by APC/CCdh1 activation in S-phase after severe replication stress'.

Nucleic acids research·2026
Same journal

VeloRM: disentangling pre- and post-splicing RNA modification dynamics at single-cell resolution.

Nucleic acids research·2026
Same journal

Accessibility of telomeric overhangs to stabilizing small-molecule ligands.

Nucleic acids research·2026
Same journal

Multivalent interactions mediate SNAIL transcription factor stimulation of the nucleosome deacetylase activity of the CoREST complex.

Nucleic acids research·2026
Same journal

Genome-wide mapping of DNA G-quadruplexes in Trypanosoma brucei chromatin reveals enrichment in coding regions and transcription start sites.

Nucleic acids research·2026
Same journal

Correction to 'The Gene Ontology knowledgebase in 2026'.

Nucleic acids research·2026
See all related articles

Related Experiment Video

Updated: Jun 5, 2026

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
05:58

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

Published on: September 6, 2024

Nucleosome accessibility governed by the dimer/tetramer interface.

Vera Böhm1, Aaron R Hieb, Andrew J Andrews

  • 1Abteilung Biophysik der Makromoleküle, Deutsches Krebsforschungszentrum, Heidelberg, Germany.

Nucleic Acids Research
|December 24, 2010
PubMed
Summary
This summary is machine-generated.

Nucleosomes pose a barrier to DNA access. We discovered a new intermediate state in nucleosome disassembly, revealing a distinct pathway for histone removal and DNA accessibility regulation.

More Related Videos

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Related Experiment Videos

Last Updated: Jun 5, 2026

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
05:58

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

Published on: September 6, 2024

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Nucleosomes, fundamental units of DNA packaging, impede enzymatic access to DNA.
  • The precise mechanisms of nucleosome disassembly remain poorly understood.
  • Understanding nucleosome dynamics is crucial for DNA replication and transcription.

Purpose of the Study:

  • To elucidate the structural intermediates and pathways involved in nucleosome disassembly.
  • To characterize a previously unrecognized structural state preceding histone dimer release.
  • To investigate the implications of nucleosome disassembly intermediates for DNA accessibility.

Main Methods:

  • Single-molecule Förster Resonance Energy Transfer (smFRET) experiments were employed.
  • smFRET was used to monitor structural changes and distances within nucleosomes.
  • Computational modeling may have been used to interpret experimental data (inferred).

Main Results:

  • A novel intermediate structural state of the nucleosome was identified before H2A-H2B dimer release.
  • This intermediate state is characterized by an increased distance between H2B and the nucleosomal dyad.
  • The proposed disassembly pathway involves opening of the tetramer/dimer interface, followed by dimer release, then tetramer removal.

Conclusions:

  • Nucleosome disassembly initiates with the opening of the (H3-H4)2 tetramer/(H2A-H2B) dimer interface.
  • The identified intermediate state is transiently populated under physiological conditions (0.2-3%).
  • These findings have significant implications for understanding in vivo histone exchange and regulation of DNA accessibility for transcription and replication machinery.