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

• Towle-Weicksel, Jamie B.

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-121505-113309

Advisor

• Adams, David S.

Year

• 2005

Sponsor

• UMass Medical School

Date created

• 2005-12-15

Localização

• Worcester

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright