Date of Award

Spring 2008

Document Type

Restricted Thesis

Terms of Use

© 2008 Benjamin Krasity. All rights reserved. Access to this work is restricted to users within the Swarthmore College network and may only be used for non-commercial, educational, and research purposes. Sharing with users outside of the Swarthmore College network is expressly prohibited. For all other uses, including reproduction and distribution, please contact the copyright holder.

Degree Name

Bachelor of Arts

Department

Biology Department

First Advisor

Amy Cheng Vollmer

Abstract

The Escherichia coli protein UspG (Universal stress protein G) is induced in response to a number of different adverse conditions, including heat shock, nutrient deprivation, and the presence of certain toxins. Its role in the survival of E. coli under stress was investigated with serial dilution experiments, which suggest that its expression under heat shock is actually harmful to the cell. β-galactosidase assays were undertaken to investigate a possible role in heat shock transcription regulation. Purification of the protein is a major focus of this study. UspG was induced from a plasmid and purified with nickel, size exclusion, and anion exchange chromatography, with favorable results. The behavior of UspG on these columns is informative of its isoelectric point and multimeric status. An investigation into a potential DNA-binding role for UspG has also begun.

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