Unpredictable chronic stress (UCS) has been established to lead to behavioral changes, insinuating that there is some underlying brain mechanism at play to induce these changes. Given the dynamic role of epigenetics in post-translational gene expression and the numerous studies identifying histone modifications within the brain under stress and learning conditions, epigenetic factors are likely the cause. Multiple publications have investigated the impact of UCS on rodent models, but few have explored the emerging zebrafish model. Zebrafish’s high level of gene homology to humans, low cost of maintenance, and predictable behavioral responses make them ideal models for these experiments. Here, we used a 14-day UCS model and examined epigenetic markers post-mortem. Western Blots and Immunohistochemistry were used to identify histone modifications in telencephalon and optic tectum while real-time PCR was used to identify mRNA levels for histone modifying enzymes.
This presentation will highlight and showcase the work/research that some of the Foley Center's most prized volunteers have done with and on behalf of the city of Prichard, Alabama. Throughout this academic year, ten Spring Hill College students (formally referred to as fellows) along with the tremendous support of Dr. Erik Goldschmidt and Dr. Demetrius Semien, engaged with several city leaders as well as with citizens of Prichard, Alabama (more specifically: Alabama Village) in order to become better informed about the major issues/concerns facing the city in addition to aspiring to dissect the mostly negative perceptions attached to the city. The fellows began their year by being trained on three different methods of assessment essential to generating and ensuring productive conversations as well as meaningful reports: Moderating for Dialogue and Deliberation (Diagnosing Wicked Problems); Need-based vs. Asset-based Community Development; and Appreciative Inquiry. Afterwards, in Prichard the fellows: spoke with a spiritual leader within the community, hosted a community meeting, spoke with the director of community development, spoke with the chief of police, spoke with the mayor, and spoke with the principal of a historical middle school located within Africatown that serves students residing in certain parts of Prichard. The fellows also attended conferences intended to nurture and improve civic engagement and involvement of which were hosted by the David Matthews Center for Civic Engagement as well as GivePulse, both of whom are partners of the Foley Fellowship program. To conclude the year, the fellows will meet with the Prichard Chamber of Commerce, and will afterwards, hold a final community meeting with citizens.
Erythromycin resistance methyltransferases (Erms) cause resistance to macrolide antibiotics by methylation of A2058 of 23S ribosomal RNA. Found in the exit tunnel of a bacterial ribosome, this position sits in the binding site for macrolide antibiotics, which interfere with nascent polypeptide extrusion to inhibit bacterial protein synthesis. Though the function and site of methylation is known for Erm enzymes, the details of enzyme-substrate interaction are still being uncovered. Structurally, Erm proteins are made of a Rossmann fold N-terminal domain connected to a C-terminal domain through a 10 amino acid linker. Using site-saturation mutagenesis, we investigated the significance of the Erm linker region in enzyme function for ErmE and ErmC.
Mitochondrial DNA is responsible for the synthesis of key metabolic proteins that allow the cell to properly regulate energy production. However, this DNA is susceptible to damage from reactive oxygen species (ROS). ROS may be produced by either endogenous or exogenous factors, and they corrupt the integrity of the mitochondrial genome, a process that is linked to cancer and other diseases. The cell has multiple ways of coping with such damage including the base excision repair pathway, which occurs in both the nucleus and mitochondria. Here, we study NEIL1, a bifunctional glycosylase that recognizes and cleaves abasic sites in replicating DNA. While NEIL1 has been well-characterized in the nucleus, its role in mitochondrial genome maintenance is less understood; however, preliminary work suggests it interacts with mitochondrial transcription factor A (TFAM). We attempt to show how these two proteins interact through purification, crystallization, and surface plasmon resonance (SPR) assays.