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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.
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Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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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.
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The Nucleosome Core Particle01:12

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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.
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Forces Acting on Chromosomes02:11

Forces Acting on Chromosomes

During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
Microtubules and motor proteins exert two types of forces on...
Forces Acting on Chromosomes02:11

Forces Acting on Chromosomes

During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
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Chromatin Packaging

Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
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In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order structures.

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Updated: Jun 23, 2026

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
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Stochastic model for nucleosome sliding under an external force.

L Mollazadeh-Beidokhti1, J Deseigne, D Lacoste

  • 1Institute for Advanced Studies in Basic Sciences (IASBS), P.O. Box 45195-1159, Zanjan 45195, Iran.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|April 28, 2009
PubMed
Summary
This summary is machine-generated.

Nucleosome sliding along DNA, driven by heat or force, is influenced by DNA mechanics and ligands. This study theoretically models directed nucleosome movement under external forces.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Genetics

Background:

  • Heat-induced nucleosome diffusion along DNA is a known phenomenon.
  • DNA mechanical properties and DNA-binding ligands significantly affect nucleosome diffusion rates.
  • A stochastic three-state model quantitatively explains observed diffusion behaviors.

Purpose of the Study:

  • To theoretically investigate the response of nucleosomes to externally applied forces inducing directed sliding.
  • To analyze how DNA mechanical properties and DNA-binding ligands modulate this force-induced nucleosome movement.

Main Methods:

  • Extension of the existing stochastic three-state model.
  • Theoretical analysis of nucleosome dynamics under external forces.

Main Results:

  • The study provides a theoretical framework for understanding directed nucleosome sliding.
  • It elucidates the interplay between external forces, DNA mechanics, and ligand presence in nucleosome positioning.

Conclusions:

  • The extended model offers insights into nucleosome positioning regulation.
  • This research lays the groundwork for future experimental studies on force-induced nucleosome dynamics.