Graduate student Andrew Hemmert in the Redinbo Group, has been selected to receive a Graduate Education Advancement Board Impact Award. This award, sponsored by the Graduate School's external advancement board of private citizens, recognizes outstanding graduate student research of particular benefit to North Carolina. The Impact Awards Selection Committee, comprised of faculty from across campus, reviewed a large number of exemplary applications. Andrew's project was selected as having exceptional quality and impact.
Andrew's research focuses on treatment options against nerve agent chemical weapons, some of the deadliest compounds ever created by man. Current treatments for nerve agent poisoning offer only limited protection and must be administered rapidly to be effective. An ideal treatment would be an intervention capable of quickly destroying a broad range of nerve agents. Andrew has developed a protein-based therapy with the enhanced ability to detoxify nerve agents up to 10,000-fold faster than current treatments. This designed protein is considered by the U.S. military to be a promising therapy candidate for nerve agent protection, and Andrew is now developing these reagents into injectable therapeutics to protect at-risk personnel, along with miniaturized detectors to alert troops to the presence of specific nerve agents. The goal of his research is to provide an array of commercial products designed to advance North Carolina's biotechnology industry and save the lives of soldiers.
As published in the Journal of Molecular Biology, in collaboration with researchers from UNC's Department of Biology, investigators in the Redinbo Group show how the majority of eukaryotic pre-mRNAs are processed by 3'-end cleavage and polyadenylation. The complex responsible contains the ~1160-residue protein Symplekin. The structure and dynamics of the Symplekin N-terminal HEAT domain were investigated to begin elucidating the role Symplekin plays in mRNA maturation. The crystal structure of the Drosophila melanogaster Symplekin HEAT domain was determined to 2.4 Å resolution with single-wavelength anomalous dispersion phasing methods.
Molecular dynamics simulations of this domain show that the presence of a unique loop dampens correlated and anticorrelated motion in the HEAT domain, therefore providing a neutral surface for potential protein–protein interactions. HEAT domains are often employed for such macromolecular contacts. Together, these data support the conclusion that the Symplekin HEAT domain serves as a scaffold for protein–protein interactions essential to the mRNA maturation process.