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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.
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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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The Nucleosome01:19

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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.
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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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The writer...
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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Related Experiment Video

Updated: Jul 23, 2025

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

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Spontaneous histone exchange between nucleosomes.

Subhra Kanti Das1, Mai Thao Huynh1, Tae-Hee Lee1

  • 1Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA.

The Journal of Biological Chemistry
|July 13, 2023
PubMed
Summary
This summary is machine-generated.

Histone H2A-H2B dimers spontaneously exchange between nucleosomes, a process crucial for chromatin stability. This dynamic histone exchange is influenced by salt concentration, acetylation, and chaperone presence, but not temperature.

Keywords:
DNA methylationhistone acetylationhistone chaperonehistone exchangenucleosomesingle-molecule FRET

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Dynamics

Background:

  • Nucleosomes, the fundamental gene-packing units in eukaryotes, consist of DNA wrapped around histone proteins.
  • Dynamic DNA-histone interactions regulate gene expression but also imply potential for nucleosome disassembly and histone exchange.
  • Spontaneous histone exchange between nucleosomes, though proposed, has not been experimentally demonstrated.

Purpose of the Study:

  • To investigate spontaneous histone exchange between nucleosomes.
  • To determine the kinetics and influencing factors of histone dimer exchange.
  • To explore the role of spontaneous histone exchange in maintaining chromatin stability.

Main Methods:

  • Utilized three-color single-molecule Förster Resonance Energy Transfer (smFRET) to monitor histone dimer dynamics.
  • Studied histone exchange at physiological nucleosome concentrations.
  • Assessed the impact of varying salt concentration, histone acetylation, temperature, DNA methylation, and histone chaperone Nap1 on exchange rates.

Main Results:

  • Demonstrated spontaneous exchange of histone H2A-H2B dimers between nucleosomes on a timescale of tens of seconds.
  • Observed increased histone exchange rates with higher monovalent salt concentration, histone acetylation, and the presence of Nap1.
  • Found no change in exchange rate with increased temperature and a decrease upon DNA methylation.

Conclusions:

  • Supports the model of histone exchange occurring through transient nucleosome disassembly.
  • Corroborates spontaneous histone diffusion within compact chromatin structures.
  • Suggests a mechanism for modulating local concentrations of histone modifications and variants, impacting chromatin regulation.