Faculty Advisor

Adams, David S.

Abstract

Vesicle trafficking is vital for the growth and life of a cell. The exocyst is an eight protein complex involved in vesicular trafficking. A model of the interactions among the exocyst proteins was proposed through yeast 2-hybrid and in vitro translation experiments, but has not been demonstrated by more stringent methods. To support these findings in vivo and to further map the binding domains, a series of immunoprecipitation experiments was performed. Green fluorescent protein (GFP) genomically tagged proteins Sec5p and Sec8p were pulled down from whole yeast lysates, and the samples were probed with anti-Sec6 antibody. If Sec6p binds Sec5-GFP or Sec8-GFP a band will appear in the western blot in the bound lane. Likewise, a similar experiment was carried out using Sec8-myc to determine its interaction with Sec6p. Results from both experiments show an in vivo interaction between Sec6p and Sec5-GFP and Sec8-GFP.

Publisher

Worcester Polytechnic Institute

Date Accepted

December 2005

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

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