The VP3 (Apoptin) protein from the Chicken Anemia Virus has been shown to selectively kill transformed cells; an activity that is dependent on subcellular localization. Studies note that Apoptin forms large multimers during this process and the role of this aggregation in cell type-specific apoptosis is unclear. Previous studies indicate that the nuclear export and multimerization activities occur via the same domain, however all current mutations affecting export also interfere with multimerization. Here we show that introduction of a point mutant (I37A) in the nuclear export sequence of Apoptin uncouples multimerization and nuclear export activities. Separation of these activities should elucidate the role of multimerization in cell type-specific apoptosis.

• 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

• DeConti, Derrick K.
• Medeiros, Adam Charles

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042208-100939

Advisor

• Wobbe, Kristin K.
• Heilman, Destin

Year

• 2008

Date created

• 2008-04-22

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright

Last modified

• 2020-12-27