Experimental manipulation of localization of the methyltransferase Suv420 at centromeres suggest that proper localization of Suv420, or its placed epigenetic marks, are critical for correct chromosome segregation during mitosis. It is suggested that it does this by indirectly regulating kinetochore-microtubule attachment. However, it remains unknown how discrete Suv420 localization to pericentromeres, and not centromeres, is achieved. Analysis of Suv420’s amino acid sequence in software to identify potential protein binding domains that are near mutations relevant to cancer predict 4 residues that may be phosphorylated by mitotic kinase Nek2. Nek2 inhibition and phosphatase inhibition of mitotically arrested retinal pigment epithelial cells containing doxycycline-induced Halo-tagged Suv420 plasmids confirm that Suv420 localization to pericentromeric chromatin during mitosis is regulated by phosphorylation. However, neither phosphomimetic mutations of Serine 20 nor Serine 355 on Suv420 were found to significantly change Suv420 localization, suggesting further tests with different Suv420 mutations and combinations of mutations is needed.

• 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

• Shell, Hannah

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042723-141015
• 106321

Advisor

• Manning, Amity L.

Year

• 2023

Date created

• 2023-04-27

Resource type

• Major Qualifying Project

Major

• Biotechnology

Source

• E-project-042723-141015

Rights statement

• In Copyright

Last modified

• 2023-06-23