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Solenoidal model for superstructure in chromatin.

J T Finch, A Klug

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1976
    PubMed
    Summary
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    Chromatin forms nucleofilaments that condense into a solenoid structure, potentially explaining X-ray reflections. Histone H1 is crucial for stabilizing this higher-order chromatin organization.

    Area of Science:

    • Molecular Biology
    • Biophysics
    • Cell Biology

    Background:

    • Chromatin, the complex of DNA and proteins that forms chromosomes within the nucleus of eukaryotic cells, is organized into higher-order structures.
    • Previous studies observed filaments and larger threads within nuclei, but their precise structure and relationship remained unclear.

    Purpose of the Study:

    • To elucidate the higher-order structure of chromatin beyond the nucleosome filament.
    • To investigate the structural basis for observed X-ray reflections in chromatin.
    • To determine the role of histone H1 in chromatin organization.

    Main Methods:

    • Electron microscopy of micrococcal nuclease-digested chromatin.
    • Biochemical extraction of chromatin components.
    • Analysis of chromatin structure in the presence of varying ionic conditions (EDTA, Mg++).

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    Main Results:

    • Chromatin appears as ~100 A diameter nucleofilaments that condense into a solenoidal structure (~110 A pitch) in the presence of Mg++.
    • X-ray reflections at 110 A are proposed to arise from the solenoid's structure, not nucleosome spacing.
    • Histone H1 is essential for solenoid stabilization, and isolated nucleosomes can form similar structures.

    Conclusions:

    • The solenoid model provides a structural basis for higher-order chromatin organization.
    • This solenoidal structure may explain observed X-ray diffraction patterns of chromatin.
    • Histone H1 plays a critical role in the formation and stabilization of the chromatin solenoid.