SUMOylation enhances DNA methyltransferase 1 activity

    Authors

    B. Lee;M. T. Muller

    Abbreviated Journal Title

    Biochem. J.

    Keywords

    DNA methylation; DNA methyltransferase 1 (DNMT1); small; ubiquitin-related modifier 1 (SUMO1); SUMOylation; ADJACENT HOMOLOGY DOMAIN; REPLICATION FOCI; IN-VIVO; SUMO MODIFICATION; DNMT1; METHYLATION; COMPLEX; PROTEIN; UBIQUITIN; GENE; Biochemistry & Molecular Biology

    Abstract

    DNA methylation regulates gene expression through Complex network of protein-protein and protein-DNA interactions in chromatin. The maintenance methylase, DNMT1 (DNA methyltransferase 1), is a prominent enzyme in the process that is linked to DNA replication and drives the heritable nature of epigenetic modifications. The mechanistic details that explain how DNMT1 catalytic action is directed and regulated in chromatin are important ill our overall understanding of gene control. In this work, we show that DNMT1 is modified by SUMOylation and we have mapped these SUMOylation sites by defined mutations. SUMOylated DNMT1 is catalytically active on genomic DNA in vivo and we find that SUMOylation significantly enhances the methylase activity of DNMT1 both in vitro and in chromatin. These data suggest that SUMOylation modulates the endogenous activity of a prominent epigenetic maintenance pathway in somatic cells.

    Journal Title

    Biochemical Journal

    Volume

    421

    Publication Date

    1-1-2009

    Document Type

    Article

    Language

    English

    First Page

    449

    Last Page

    461

    WOS Identifier

    WOS:000268615900013

    ISSN

    0264-6021

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