Student Work

Exploring the Interactions of Yeast Exocyst Complex Proteins Using Immunoprecipitation Experiments

Public

Downloadable Content

open in viewer

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.

  • 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
Publisher
Identifier
  • E-project-121505-113309
Advisor
Year
  • 2005
Sponsor
Date created
  • 2005-12-15
Location
  • Worcester
Resource type
Major
Rights statement

Relations

In Collection:

Items

Items

Permanent link to this page: https://digital.wpi.edu/show/mc87pr83x