Structure and Biochemical Activities of Escherichia coli MgsA

Current position: Ph.D. student, Department of Biochemistry, University of Wisconsin-Madison

Education: Bachelor of Science in Biochemistry (2007), University of Maryland, College Park

Nonscientific interests: Playing basketball and hiking

In my undergraduate studies I became interested in protein biochemistry and elucidating the roles of proteins in cellular pathways. Upon entering the University of Wisconsin-Madison, I joined Mike Cox's laboratory because it offered the opportunity to study proteins at the interface of DNA replication, recombination, and repair. These processes were intriguing to me because they are central to all forms of life and are coordinated in fascinating ways.

I was interested in studying the MgsA protein because although genetic studies indicated that it functions in cellular responses to stalled replication forks, structural and biochemical studies were severely lacking. I also saw the opportunity to gain exposure to techniques spanning molecular biology, biochemistry, and structural biology while addressing a basic scientific question. We used x-ray crystallography to solve the structure of MgsA and tandem affinity purification to identify a novel MgsA interaction partner. These findings provide insights into the MgsA family of proteins, which are detailed in this publication.