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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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.
Writers
The writer...
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Chromatin Packaging02:21

Chromatin Packaging

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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
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...
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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
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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Condensins02:15

Condensins

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Condensins are large protein complexes that use ATP to fuel the assembly of chromosomes during mitosis. They transform the tangled, shapeless mass of post-interphase DNA into individualized chromosomes by compacting, organizing, and segregating chromosomal DNA.
The plant and animal cells contain two types of condensin complexes—condensin I and condensin II. Both complexes have five subunits: two SMC (Structural Maintenance of Chromosomes) subunits, a kleisin subunit, and two HEAT-repeat...
3.7K
Euchromatin01:01

Euchromatin

7.6K
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
7.6K
Chromatin Position Affects Gene Expression02:35

Chromatin Position Affects Gene Expression

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Chromatin is the massive complex of DNA and proteins packaged inside the nucleus. The complexity of chromatin folding and how it is packaged inside the nucleus greatly influences  access to genetic information. Generally, the nucleus' periphery is considered transcriptionally repressive, while the cell's interior is considered a transcriptionally active area. 
Topologically Associated Domains (TADs)
The 3-dimensional positioning of chromatin in the nucleus influences the...
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Related Experiment Video

Updated: Sep 15, 2025

Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA
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Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA

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Condensate-driven chromatin organization via elastocapillary interactions.

Hongbo Zhao, Amy R Strom, Jorine M Eeftens

    Biorxiv : the Preprint Server for Biology
    |July 15, 2025
    PubMed
    Summary
    This summary is machine-generated.

    Nuclear condensates and chromatin are interdependent, with phase separation physics governing their interactions. This study reveals how wetting properties and chromatin stiffness shape condensate morphology and function.

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    Area of Science:

    • Cell Biology
    • Biophysics
    • Genomics

    Background:

    • Biomolecular condensates are crucial for genome organization and function within eukaryotic cells.
    • Nuclear condensates, formed by proteins and RNA, exhibit diverse morphologies driven by phase separation around chromatin.
    • The physical principles governing condensate-chromatin interactions and their impact on genome organization are not fully understood.

    Purpose of the Study:

    • To develop and validate a mesoscopic model integrating phase separation physics and chromatin mechanics.
    • To investigate the roles of wetting properties and chromatin stiffness in shaping nuclear condensate morphology.
    • To elucidate the reciprocal relationship between condensates and chromatin mechanics.

    Main Methods:

    • Computational modeling combined with experimental validation.
    • Utilized canonical condensate proteins: heterochromatin protein 1 alpha (HP1α) and bromodomain-containing protein 4 (BRD4).
    • Investigated condensate morphology, wetting properties, and chromatin mechanics.

    Main Results:

    • Wetting properties and chromatin stiffness dictate condensate morphology.
    • Nuclear condensates actively remodel chromatin mechanics and organization.
    • Elastocapillarity governs the interplay between condensate interfacial tension and chromatin deformation, explaining emergent behaviors beyond simple liquid-liquid phase separation (LLPS).

    Conclusions:

    • Nuclear condensates and chromatin exhibit a fundamental interdependence.
    • Biomolecular wetting properties significantly influence genome organization, transcriptional regulation, and epigenetic control.
    • The developed model and methodologies offer a generalizable framework for studying multiphase soft matter systems in biological and synthetic contexts.