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Nuclear matrix-associated DNA methylase.

R H Burdon, M Qureshi, R L Adams

    Biochimica Et Biophysica Acta
    |May 24, 1985
    PubMed
    Summary
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    Researchers identified a bound form of DNA methylase (EC 2.1.1.37) in mouse cells, distinct from the soluble form. This bound enzyme, associated with nuclear structures, can be released and exhibits similar properties to the soluble DNA methylase.

    Area of Science:

    • Molecular Biology
    • Enzymology
    • Cell Biology

    Background:

    • DNA methylase (EC 2.1.1.37) is crucial for epigenetic regulation.
    • Previous studies primarily focused on soluble DNA methylase extracted using 0.2M NaCl buffers.
    • A significant portion of DNA methylase activity exists in a bound form within the nucleus.

    Purpose of the Study:

    • To characterize the 'bound' form of DNA methylase.
    • To investigate the association of DNA methylase with nuclear structures.
    • To compare the properties of the bound and soluble DNA methylase forms.

    Main Methods:

    • Extraction of nuclear proteins from mouse ascites cells.
    • Differential salt extraction to separate soluble and bound enzyme fractions.

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  • Disruption of enzyme-bound complexes using high ammonium sulphate concentrations.
  • Enzymatic assays to determine DNA methylase activity and properties.

    • Main Results:

    • A 'bound' DNA methylase fraction was identified, associated with 2 M NaCl-resistant nuclear matrix-like structures.
    • This association is partially dependent on ongoing DNA replication and protein synthesis.
    • The bound DNA methylase could be solubilized in vitro using high ammonium sulphate concentrations.
    • Enzymic properties of the bound DNA methylase were found to be similar to the soluble form.

    Conclusions:

    • Mouse ascites cell nuclei contain both soluble and bound forms of DNA methylase.
    • The bound DNA methylase is associated with nuclear matrix components and its release is dependent on specific conditions.
    • The bound and soluble DNA methylase forms share similar enzymatic characteristics, suggesting a common functional role.