Faculty Advisor

Adams, David S.

Center

University of Massachusetts Medical Center

Abstract

Eukaryotic vesicle targeting and fusion are conserved processes that involve SNARE and SM proteins. The SM protein Sly1 and its cognate SNARE Sed5 function in trafficking between the ER and the Golgi. It is known that Sly1 binds to the N-terminal peptide of Sed5. To investigate an alternative binding, a truncated Sed5 construct, Sed5 (23-324), was designed. This construct was cloned, expressed in E. coli and S. cerevisiae, and purified. Binding studies were conducted and the results indicated that the truncated Sed5 (23-324) did not bind to Sly1, suggesting that the N-terminal binding site may be the only binding domain.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2012

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

Advisor Program

Biology and Biotechnology

Project Center

University of Massachusetts Medical Center

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