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MORC2 phosphorylation fine tunes its DNA compaction activity

Winnie Tan, Jeong Veen Park, Hariprasad Venugopal

    Biorxiv : the Preprint Server for Biology
    |July 9, 2024
    PubMed

    Insights

    MORC2, a chromatin remodelling ATPase, compacts DNA to remodel chromatin, influenced by phosphorylation. This mechanism, crucial for DNA repair and cancer, offers a potential therapeutic target.

    Area of Science:

    • Molecular biology
    • Epigenetics
    • Cancer research

    Background:

    • MORC2 is an oncoprotein involved in epigenetic regulation and DNA damage response.
    • The C-terminal domain (CTD) of MORC2 is phosphorylated during DNA damage and promotes cancer, but its role in chromatin remodeling is unknown.

    Purpose of the Study:

    • To characterize the molecular function of phosphorylated MORC2 in chromatin remodeling.
    • To investigate the role of MORC2's CTD phosphorylation in its DNA binding and ATPase activity.

    Main Methods:

    • Biochemical assays to characterize full-length phosphorylated MORC2.
    • Structural analysis of MORC2-DNA interactions.
    • In vitro assays to assess chromatin remodeling activity.

    Main Results:

    • MORC2 binds preferentially to open chromatin and functions as a DNA sliding clamp.
    • A specific motif in the CTD mediates ATP hydrolysis and cooperative DNA binding.
    • MORC2 induces ATP hydrolysis-dependent DNA compaction, remodeling chromatin.
    • Phosphorylation of MORC2 CTD regulates its chromatin remodeling activity.

    Conclusions:

    • MORC2's phosphorylation state is a key regulator of its chromatin remodeling function.
    • MORC2-mediated DNA compaction is a novel mechanism for chromatin remodeling.
    • Phosphorylated MORC2 CTD represents a potential therapeutic target for cancer treatment.

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