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Nucleosome core particle structure and structural changes in solution.

K O Greulich, J Ausio, H Eisenberg

    Journal of Molecular Biology
    |November 5, 1985
    PubMed
    Summary
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    The radius of gyration for chicken erythrocyte nucleosome core particles was determined using small-angle X-ray scattering. This study also investigated particle hydration and volume using equilibrium sedimentation.

    Area of Science:

    • Structural biology
    • Biophysics
    • Nucleosome structure

    Background:

    • Nucleosome core particles (NCPs) are fundamental units of DNA packaging in eukaryotes.
    • Understanding NCP structure and interactions is crucial for comprehending gene regulation.
    • Previous studies have explored NCP dimensions, but hydration and volume require further elucidation.

    Purpose of the Study:

    • To determine the radius of gyration (Rg) of chicken erythrocyte nucleosome core particles.
    • To investigate the influence of salt and particle concentration on NCP dimensions.
    • To estimate NCP hydration and total particle volume.

    Main Methods:

    • Small-angle X-ray scattering (SAXS) was used to measure the radius of gyration.
    • Particle concentration dependence analysis was performed using SAXS.

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  • Equilibrium sedimentation with density contrast variation was employed to assess hydration and volume, utilizing sucrose and gamma-cyclodextrin as probes.

    • Main Results:

    • The radius of gyration (Rg) was determined to be 4.56 ± 0.07 nm, independent of particle and NaCl concentrations (0.1–0.6 M).
    • A large, positive second virial coefficient (A2) suggests long-range, non-electrostatic repulsive ordering.
    • Equilibrium sedimentation provided estimates for core particle hydration and total particle volume.

    Conclusions:

    • Chicken erythrocyte nucleosome core particles exhibit a stable radius of gyration under varying ionic conditions.
    • Non-electrostatic interactions likely govern the solution behavior of these particles.
    • The study provides valuable insights into the hydration and volumetric properties of nucleosome core particles.