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Related Concept Videos

Nucleosome Remodeling02:54

Nucleosome Remodeling

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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
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Chromatin Packaging02:21

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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? 
The chromatin
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Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...
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The process of chromosome duplication during cell division requires genome-wide disruption and re-assembly of chromatin. The chromatin structure must be accurately inherited, reassembled, and maintained in the daughter cells to ensure lineage propagation.
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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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Updated: Oct 29, 2025

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Tetranucleosome Interactions Drive Chromatin Folding.

Walter Alvarado1, Joshua Moller2, Andrew L Ferguson2

  • 1Biophysical Sciences, University of Chicago, Chicago, Illinois 60637 United States.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Genomics

Background:

  • Chromatin's multiscale organization regulates gene expression via genome condensation and expansion.
  • Understanding the thermodynamic stability of mesoscopic chromatin structures is crucial but incomplete.

Purpose of the Study:

  • To identify and characterize the structure and free energy of metastable states in short chromatin segments.
  • To investigate the role of tetranucleosome conformations in DNA accessibility and chromatin dynamics.

Main Methods:

  • Utilized molecular modeling with the 1CPN mesoscale model of chromatin.
  • Employed nonlinear manifold learning to analyze chromatin segments (4-16 nucleosomes).

Main Results:

  • Identified stable "α-tetrahedron" and "β-rhombus" tetranucleosome conformations.
  • Observed that increased nucleosome repeat length leads to liquid-like dynamic behavior.
  • Found tetranucleosome motifs to be intrinsically stable, driven by local internucleosomal interactions.

Conclusions:

  • Tetranucleosome motifs are key to chromatin packing, dynamics, and accessibility.
  • Emergent local mesoscale structures significantly influence chromatin behavior.
  • Findings explain slow nucleosome dynamics and provide a mechanistic picture of chromatin organization.