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Related Experiment Videos

Salt-induced structural changes in nucleosomes

G Russev, L Vassilev, R Tsanev

    Molecular Biology Reports
    |March 31, 1980
    PubMed
    Summary

    Nucleosomes undergo a reversible structural change before dissociating, involving DNA end detachment from the protein core. This transition is salt-dependent and suggests specific protein-DNA binding interactions within the nucleosome structure.

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    Dynamics of association of origins of DNA replication with the nuclear matrix during the cell cycle.

    Nucleic acids research·2001

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Structural Biology

    Background:

    • Nucleosomes are the basic units of DNA packaging in eukaryotes.
    • Understanding nucleosome stability and structural transitions is crucial for comprehending DNA accessibility and gene regulation.

    Purpose of the Study:

    • To investigate the structural changes and dissociation mechanisms of Ehrlich ascites tumor (EAT) nucleosomes under varying salt concentrations.
    • To elucidate the nature of the interaction between DNA and the protein core within nucleosomes.

    Main Methods:

    • Sucrose density gradient centrifugation to analyze nucleosome behavior.
    • Electron microscopy to visualize structural alterations.
    • Varying sodium chloride (NaCl) concentrations to induce dissociation and structural transitions.

    Main Results:

    • Nucleosomes exhibited a decrease in sedimentation coefficient from 11S to 8S between 0.6M-1M NaCl, indicating a structural transition.
    • This transition was reversible and not due to protein loss, involving the detachment of nucleosomal DNA ends from the protein core.
    • Complete dissociation into free DNA and protein occurred at higher NaCl concentrations (0.6M-1.5M).

    Conclusions:

    • Nucleosomes undergo a reversible structural transition involving DNA end detachment prior to complete protein-DNA dissociation.
    • This transition suggests differential binding affinities within the nucleosome, with arginine-rich domains potentially binding the central DNA more tightly than lysine-rich domains bind the DNA ends.

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