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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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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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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Spontaneous Histone Exchange Between Nucleosomes.

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    Biorxiv : the Preprint Server for Biology
    |May 22, 2023
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    Summary
    This summary is machine-generated.

    Histones spontaneously exchange between nucleosomes, a process crucial for chromatin stability. This dynamic histone exchange occurs within tens of seconds and is influenced by salt concentration, acetylation, and chaperone presence.

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    Area of Science:

    • Molecular Biology
    • Epigenetics
    • Biophysics

    Background:

    • Nucleosomes, the fundamental units of eukaryotic DNA packaging, consist of DNA wrapped around a histone protein core.
    • Dynamic DNA-histone interactions regulate gene expression, implying transient nucleosome disassembly.
    • Spontaneous histone exchange between nucleosomes, though unproven, is hypothesized to maintain chromatin stability.

    Approach:

    • Utilized three-color single-molecule Förster Resonance Energy Transfer (smFRET) to monitor histone dimer dynamics.
    • Investigated histone H2A-H2B dimer exchange between nucleosomes at physiological concentrations.
    • Assessed the influence of salt concentration, histone acetylation, temperature, DNA methylation, and histone chaperone Nap1 on exchange rates.

    Key Points:

    • Demonstrated spontaneous exchange of histone H2A-H2B dimers between nucleosomes on a timescale of tens of seconds.
    • Exchange rate increases with higher monovalent salt concentration and histone acetylation.
    • Histone exchange is accelerated by the histone chaperone Nap1 but unaffected by temperature; it decreases with DNA methylation.

    Conclusions:

    • Supports a model of histone exchange through transient, repetitive partial nucleosome disassembly.
    • Corroborates spontaneous histone diffusion within compact chromatin structures.
    • Highlights the role of histone exchange in modulating local histone modifications and variants, impacting gene regulation.