Nicholas Grossoehme, Ph.D.
College of Arts and Sciences
Chemistry, Physics and Geology
Sufficient concentrations of metal within a cell are required for proper cellular function; however, metals become toxic at very high concentrations. Therefore, it is important for an organism to have a mechanism for maintaining metal homeostasis within its cells. Streptomyces coelicolor, a soil-dwelling bacterium important in the production of antibiotics, utilizes the nickel uptake regulator (NUR) to maintain nickel homeostasis and oxidative response. NUR functions as a transcriptional repressor that responds to changing cytosolic concentrations of Ni2+. Previous research describes two key metal-binding sites per NUR monomer. Our research seeks to analyze how changes to these binding sites affect the ability of NUR to coordinate metals and bind to DNA. NUR mutants containing single or multiple amino acid substitutions at each binding site were cloned. Biophysical characterization of these mutants and the wild-type protein will aid in understanding the role each metal site plays in the function of NUR.
Manley, Olivia and Grossoehme, Nick E.
"Cloning and characterization of nickel uptake regulator NUR mutants from Streptomyces coelicolor,"
The Winthrop McNair Research Bulletin: Vol. 1, Article 9.
Available at: https://digitalcommons.winthrop.edu/wmrb/vol1/iss1/9