Faculty Advisor

Adams, David S.

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2010

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

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