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.

• 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

• Zeeb, Kristine Marie

Contributors

• Munson, Mary

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042412-200404

Advisor

• Adams, David S.

Year

• 2012

Sponsor

• UMass Medical School

Date created

• 2012-04-24

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright

Last modified

• 2023-09-28