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Related Experiment Videos

Conformational changes of the chromatin subunit.

V C Gordon, C M Knobler, D E Olins

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1978
    PubMed
    Summary

    Hydrodynamic studies reveal two salt-dependent conformational transitions in monomer chromatin subunits (v1). These changes, observed across varying ionic strengths, suggest alterations in the frictional coefficient rather than molecular weight.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Biophysics

    Background:

    • Chromatin subunits (v1) are fundamental units of DNA packaging.
    • Understanding their structural dynamics is crucial for gene regulation.
    • Ionic strength significantly influences macromolecular interactions.

    Purpose of the Study:

    • To investigate the conformational changes of monomer chromatin subunits (v1) under varying ionic strengths.
    • To determine the impact of ionic strength on hydrodynamic properties such as sedimentation coefficient (s20,w) and diffusion coefficient (D20,w).

    Main Methods:

    • Hydrodynamic studies using analytical ultracentrifugation.
    • Measurements of sedimentation coefficient (s20,w) and diffusion coefficient (D20,w).
    • Experiments conducted across a range of ionic strengths (0.7 mM to 100 mM KCl).

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  • Crosslinking with formaldehyde to assess structural stability.

    • Main Results:

    • Two distinct salt-dependent conformational transitions were identified at approximately 7.5 mM and 1 mM ionic strength.
    • A decrease in ionic strength from 10 mM to 5 mM resulted in reduced s20,w and D20,w values for v1.
    • Formaldehyde-crosslinked v1 did not exhibit similar salt-dependent hydrodynamic changes.
    • Molecular weight remained constant, indicating changes in frictional coefficient.

    Conclusions:

    • Monomer chromatin subunits (v1) undergo significant conformational transitions in response to ionic strength.
    • These transitions are primarily attributed to alterations in the frictional coefficient, not molecular weight.
    • The findings provide insights into the dynamic nature of chromatin structure and its response to physiological ionic conditions.