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Intermolecular histone H4 interactions in core nucleosomes.

D G Chung, P N Lewis

    Biochemistry
    |April 22, 1986
    PubMed
    Summary

    Synthetic nucleosomes with pyrene-labeled histone H4 (H4) show close proximity of H4 molecules. Ionic strength changes reveal cooperative disruption of these structures.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • Nucleosomes are fundamental units of DNA packaging in eukaryotes.
    • Histone modifications play crucial roles in gene regulation and chromatin structure.
    • Fluorescent labeling is a powerful tool for studying molecular interactions and dynamics.

    Purpose of the Study:

    • To synthesize and characterize pyrene-labeled nucleosome-like particles.
    • To investigate the proximity of histone H4 (H4) molecules within reconstituted nucleosomes using pyrene excimer fluorescence.
    • To examine the effect of ionic strength on nucleosome structure and H4-H4 interactions.

    Main Methods:

    • Reconstitution of nucleosome-like particles using chicken histone H4 labeled with 1-N-pyrenyliodoacetamide at methionine-84.
    • Incorporation of randomly lysine-labeled H4 with a dual-pyrene moiety to create an intramolecular excimer standard.
    • Analysis of pyrene excimer fluorescence properties as a function of ionic strength (NaCl concentration).
    • Monitoring changes in accessibility and environment polarity using other fluors.

    Main Results:

    • Synthetic nucleosomes with pyrene-labeled H4 exhibited properties similar to native particles.
    • The pyrene excimer fluorescence indicated close proximity of the two H4 molecules in the reconstituted particle.
    • A cooperative disruption of the H4-H4 pyrene excimer fluorescence was observed around 0.1 M NaCl.
    • This disruption preceded changes in accessibility and polarity, suggesting a specific structural event.

    Conclusions:

    • Pyrene labeling provides a sensitive method to probe histone H4 proximity in nucleosomes.
    • The study demonstrates a cooperative structural transition in nucleosome-like particles as a function of ionic strength.
    • The findings highlight the dynamic nature of nucleosome structure and histone-histone interactions.

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