Presenter: Alexander Benbrook
Authors: Alexander Benbrook
Faculty Advisor: Jeffery Tessem
Institution: Brigham Young University
Diabetes is a growing concern in the world, 1 in 10 Americans have been diagnosed and that number is expected to grow over the next few years. Research has shown the orphan nuclear receptor protein receptor Nr4a1 to be one gene that is a promising target for Diabetes[1]. Nr4a1 has been shown to play key roles in carbohydrate and lipid metabolism and energy homeostasis and has been shown to play a key role in diabetes pathogenesis[2]. In diabetes, individuals show elevated levels of glucose and elevated levels of free fatty acids[3]. Fatty acids interfere with Nr41 binding[4]. Our goal is to better understand fatty acid interactions with Nr4a1 using an electrophoretic mobility shift assay (EMSA) a technique that uses fluorescently labeled DNA primers that Nr4a1 binds to, creating a protein-DNA complex. We looked at the effect of saturation versus unsaturation on interacting with Nr4a1 binding. Subsequently we explored the degree of saturation on Nr4a1 binding. Here we present the effect of saturation and degree of saturation on modulating Nr4a1 binding to its DNA binding motif.