The interaction of the exocyst complex and SNARE proteins is essential in exocytosis, specifically to the tethering and fusion of secretory vesicles at the plasma membrane. While the specific mechanisms of vesicle trafficking are largely unknown, direct interactions have been found between the exocyst subunit Sec6p and the t-SNARE Sec9p. To investigate a possible binding site for the two proteins, a recombinant S. cerevisiae Sec9p mutant was cloned, expressed in E. coli, and purified. Binding studies, including gel filtration and gel shift assays, were conducted. The results indicate that the mutations tested did not disrupt binding of the proteins of interest. Future work should include examination of other possible binding sites in Sec9p.

• 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

• Wood, Ashleigh Elizabeth

Contributors

• Munson, Mary

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042710-125522

Advisor

• Adams, David S.

Year

• 2010

Sponsor

• UMass Medical School

Date created

• 2010-04-27

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright

Last modified

• 2023-09-28