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The Nucleosome Core Particle

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 Particle

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...

Nucleosome Remodeling

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

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...

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Related Experiment Video

Updated: Jun 25, 2026

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

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

Published on: January 31, 2019

DNA sequence-dependent variation in nucleosome structure, stability, and dynamics detected by a FRET-based analysis.

L Kelbauskas¹, N Woodbury, D Lohr

¹Biodesign Institute, Arizona State University, Tempe, AZ 85287, USA. laimonas.kelbauskas@asu.edu

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire

|February 24, 2009

Summary

Förster resonance energy transfer (FRET) reveals distinct DNA sequence-dependent structures and dynamics in nucleosomes. Specific nucleosome types, like 5S rDNA, show enhanced stability compared to MMTV-B and GAL10, impacting genetic regulation.

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

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Analyzing and Building Nucleic Acid Structures with 3DNA

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Area of Science:

Biophysics
Molecular Biology
Genetics

Background:

Nucleosomes, the basic units of DNA packaging, regulate access to genetic material.
Förster resonance energy transfer (FRET) is a powerful technique for studying biomolecular conformational changes.
Understanding nucleosome dynamics is crucial for gene regulation and cellular processes.

Purpose of the Study:

To compare DNA sequence-dependent structural, stability, and dynamic differences among various nucleosome types using FRET.
To investigate the influence of DNA sequence on nucleosome stability and dynamics.
To explore the role of nucleosome structure and dynamics in facilitating targeted DNA accessibility for regulatory factors.

Main Methods:

Utilized Förster resonance energy transfer (FRET) techniques to analyze nucleosome conformational features.
Compared FRET-based studies of the 5S rDNA nucleosome standard with promoter-derived nucleosomes (MMTV-B and GAL10).
Examined H2A/H2B-depleted nucleosomal particles to assess the impact of histone variants.

Main Results:

Detected significant DNA sequence-dependent variations in nucleosome structure, stability, and dynamics.
Observed enhanced stability and diminished DNA dynamics in 5S nucleosomes and their depleted particles compared to MMTV-B and GAL10.
Identified significant location-dependent (intranucleosomal) variations in stability and dynamics, which differ among nucleosome types.

Conclusions:

DNA sequence significantly influences nucleosome structure, stability, and dynamics.
Nucleosome type and composition (e.g., presence of H2A/H2B) critically affect these properties.
Variations in nucleosome dynamics and stability can facilitate targeted DNA accessibility, aiding in the regulation of genetic processes.