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 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 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 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 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...

You might also read

Related Articles

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

Sort by
Same author

Mechanisms of stimulation of SAGA-mediated nucleosome acetylation by a transcriptional activator.

Biochemistry and biophysics reports·2021
Same author

Distinct requirements of linker DNA and transcriptional activators in promoting SAGA-mediated nucleosome acetylation.

The Journal of biological chemistry·2018
Same author

Chemical Genetic Analysis of Protein Kinase Cascades.

TheScientificWorldJournal·2018
Same author

Structure, High Affinity, and Negative Cooperativity of the Escherichia coli Holo-(Acyl Carrier Protein):Holo-(Acyl Carrier Protein) Synthase Complex.

Journal of molecular biology·2017
Same author

Solid-phase synthesis of highly repetitive chromatin assembly templates.

Analytical biochemistry·2017
Same author

Expression and purification of histone H3 proteins containing multiple sites of lysine acetylation using nonsense suppression.

Protein expression and purification·2015
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 9, 2026

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

Nucleosome interactions and stability in an ordered nucleosome array model system.

Melissa J Blacketer1, Sarah J Feely, Michael A Shogren-Knaak

  • 1Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.

The Journal of Biological Chemistry
|August 27, 2010
PubMed
Summary
This summary is machine-generated.

Short DNA arrays (nucleosome chains) show self-association and increased stability. Even small chains of two nucleosomes interact, suggesting short DNA segments contribute to complex fiber interactions and protect against histone loss.

More Related Videos

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

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

Related Experiment Videos

Last Updated: Jun 9, 2026

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

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

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

Area of Science:

  • Molecular Biology
  • Genetics
  • Biophysics

Background:

  • Eukaryotic DNA is primarily organized into nucleosomes, but higher-order structures and nucleosome stability dynamics remain unclear.
  • Understanding nucleosome interactions is crucial for comprehending DNA packaging and regulation.

Purpose of the Study:

  • To investigate the structural and functional roles of individual nucleosomal sites.
  • To characterize the higher-order structure and stability of short nucleosome arrays.

Main Methods:

  • Development of a chromatin model system with 1-4 ligated mononucleosomes.
  • Systematic variation of array composition, saturation, and length.
  • Analysis of intra-array compaction and inter-array self-association.

Main Results:

  • Tetranucleosomal arrays exhibit intra-array compaction, but it's less extensive and histone H4 tail-independent compared to longer arrays.
  • Nucleosome arrays demonstrate cooperative self-association, decreasing with reduced H4 tail presence.
  • Even short arrays (dinucleosomes) show significant self-association, indicating minimal determinants for inter-array interactions.
  • Nucleosome stability increases with array length and saturation, suggesting protection against histone ejection.

Conclusions:

  • Short nucleosome arrays (≤4 nucleosomes) do not fully compact into the 30-nm fiber.
  • Relatively few nucleosomal interactions are required for inter-array association, implying short DNA segments contribute to complex fiber interactions in vivo.
  • Ordered and saturated nucleosome arrays likely protect DNA regions from histone loss in vivo.