Epigenetic regulation of histones through phosphorylation, methylation, and acetylation is crucial for regulating chromosome organization and gene expression. The histone methyltransferase Suv420H2 is responsible for placing di- and tri- methyl marks on the lysine 20 residue of histone 4. H4K20me2/3 is a repressive mark that is enriched at centromeres and telomeres, as well as at silenced genes and its loss or misplacement can compromise gene expression, repair of DNA damage, and chromosome segregation during mitosis. However, the mechanism that regulates the localization and activity of Suv420 is not well understood. Motif analysis performed with the database ELM identified putative binding motifs for several kinases and phosphatases, including the mitotic kinase Nek2. In this project, I have tested the hypothesis that, during mitosis, the association of Suv420H2 with chromatin is regulated by the Nek2 kinase. I have used cell fractionation assays and immunofluorescence imaging of cells to monitor the subcellular localization of Suv420H2 in control mitotic cells and those following inhibition of Nek2 or protein phosphatase I (PP1). My data indicate that the localization of Suv420H2 in mitosis is sensitive to its phosphorylation state.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Lee, Stephanie

Publisher

• Worcester Polytechnic Institute

Identifier

• 121782
• E-project-042524-150706

Keyword

• Chromosome Segregation
• Suv420
• Cancer
• Epigenetics

Advisor

• Manning, Amity L.

Year

• 2024

Date created

• 2024-04-25

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Source

• E-project-042524-150706

Rights statement

• In Copyright