Histone H4 lysine 20 methyltransferase SUV4-20H2 regulates mitotic fidelity

Hahn, Sabine

Etd

Histone H4 lysine 20 methyltransferase SUV4-20H2 regulates mitotic fidelity

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Dynamic regulation of chromatin structure is critical for a number of biological processes, including accurate chromosome segregation during mitosis. Much of this regulation is accomplished through epigenetic mechanisms that include, but are not limited to DNA methylation and various histone post-translational modifications. During cell division, epigenetic mechanisms influence the formation and function of the centromere and, ultimately, the kinetochore that are responsible for linking chromosomes to the mitotic spindle. Defects in this regulation corrupt the way attachments are made and can result in chromosome segregation errors. Here I characterize the role of the SUV4-20H2, a histone lysine methyltransferase, in regulating centromere structure and kinetochore composition. My data indicate that SUV4-20H2 itself and its methyltransferase activity are tightly regulated throughout the cell cycle and its misregulation is implicated in disease such that increases in centromeric Histone 4 Lysine 20 (H4K20) trimethylation induced by tethering SUV4-20H2 to the centromere limits Aurora B localization to the centromere and, ultimately, promotes segregation errors.

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