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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 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...

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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

Single-pair FRET experiments on nucleosome conformational dynamics.

Ruth Buning1, John van Noort

  • 1Physics of Life Processes, LION, Leiden University, Niels Bohrweg 2, 2333 CA Leiden, The Netherlands. buning@physics.leidenuniv.nl

Biochimie
|August 31, 2010
PubMed
Summary

Single nucleosome dynamics are revealed by single-molecule FRET techniques. These studies show nucleosomes are highly dynamic, influenced by histone modifications and DNA sequence, impacting DNA accessibility.

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Last Updated: Jun 9, 2026

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

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

Area of Science:

  • Molecular Biology
  • Biophysics
  • Genetics

Background:

  • Nucleosomes are fundamental units of DNA organization in eukaryotes.
  • They regulate DNA-related processes like transcription, replication, and repair.
  • Nucleosome dynamics, such as DNA breathing, control DNA accessibility.

Purpose of the Study:

  • To review single-molecule FRET studies on nucleosome conformational dynamics.
  • To highlight the dynamic nature of nucleosomes and factors influencing it.

Main Methods:

  • Single-pair Fluorescence Resonance Energy Transfer (spFRET) microscopy.
  • Fluorescence Correlation Spectroscopy (FCS).
  • Confocal and widefield TIRF microscopy on freely diffusing and immobilized nucleosomes.

Main Results:

  • spFRET experiments reveal highly dynamic nucleosome organization.
  • Nucleosome dynamics are modulated by histone post-translational modifications.
  • DNA sequence also influences nucleosome conformational dynamics.

Conclusions:

  • Single nucleosome studies provide detailed insights into DNA accessibility regulation.
  • Nucleosome dynamics are complex and influenced by multiple factors.
  • Understanding these dynamics is key to comprehending DNA-templated processes.