Abstract
Glutaredoxins are enzymes that, among other things, protect the cell from oxidative stress damage by reducing disulfide bonds in proteins. In order to understand more about the proteins these enzymes partner with, we treated yeast expressing tagged forms of these glutaredoxins with divinyl sulfone (DVSF), a chemical crosslinker. What we found was that when treated with DVSF, Grx2, Grx3, Grx4, and Grx7 formed a laddering pattern when examined with a Western Blot. This is compared to controls treated with an equivalent dose of DMSO, which formed a single band at the expected molecular weight. Our results indicate that DVSF caused the glutaredoxins to form crosslinks with other proteins, which is why they displayed bands at several different molecular weights. As this method of chemical crosslinking has been used to study similar enzymes, these results open up promising new areas of research related to the glutaredoxins’ protein partners.
Advisor
West, James
Department
Biology
Recommended Citation
Oliver, Lily G., "S. cerevisiae Glutaredoxins Are Targets of the Protein Crosslinker Divinyl Sulfone" (2025). Senior Independent Study Theses. Paper 13465.
https://openworks.wooster.edu/independentstudy/13465
Publication Date
2025
Degree Granted
Bachelor of Arts
Document Type
Senior Independent Study Thesis
© Copyright 2025 Lily G. Oliver