Faculty Advisor

Heilman, Destin

Faculty Advisor

Wobbe, Kristin K

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2008

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Chemistry and Biochemistry

Advisor Department

BC

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