Danica Maile
Ravi Maisuria
Chemistry College of Science and Engineering May 2018 Mentor: Erin Carlson Mentor's Department: Chemistry
Psychology, Chemistry College of Biological Sciences, College of Liberal Arts May 2019 Mentor: G.W. Gant Luxton Mentor's Department: Genetics, Cell Biology, and Development
A Search for Antibacterial Agents through Soil Sample Screening
The Relationship Between LAP1 and LINC Complexes with Varying Substrate Stiffness to Identify TorsinA’s Role in Mechanotransduction
Currently, there has been a devastating increase in antibiotic resistant infections due to bacteria's rapid replication time and adaptability. Because of this, new antibiotics are greatly needed. The Carlson Lab works to develop novel antibacterial compounds through the examination and characterization of novel bioactive natural products produced by microorganisms which are extensively used as commercial antibiotics. This poster will outline how soil samples from northern Wisconsin and Minnesota were screened for organisms of interest based on unusual phenotypes and antagonistic inter-organismal interactions. These organisms were used to create a microbial library of lead organisms. We have worked to trigger the production of novel secondary metabolites by culturing an organism of interest alongside the other organisms in the library to attempt to activate natural product gene clusters not active in pure culture. This was seen in three different organisms which were then analyzed via mass spectrometry. Looking forward, further mass spectrometry, NMR, and DNA sequencing can be utilized to further characterize and identify novel compounds and the organisms of interest.
Torsin ATPases are part of the AAA+ family and contribute to a variety of cellular activities. Though similar, Torsins are considered outliers of the family due to their diverse and unique characteristics. Specifically, TorsinA is an important member of the family and is involved with cellular architecture and nuclear movement regulation. The most common mutation of TorsinA is TorsinAΔE. This mutation is directly responsible for dystonia (DYT1). Furthermore, TorsinAΔE has been seen to compromise the nuclear envelope (NE) and cytoskeleton filaments which, ultimately, have been shown to interfere with neurotic networks. Proper functioning of TorsinA is mediated by its cofactors: lamina-associated polypeptide 1 (LAP1), LULL1 (luminal domain-like LAP-1) along with linker of nucleoskeleton and cytoskeleton (LINC) complexes, which are comprised of Nesprin proteins. In regards to neurotic networks and associated neurodegeneration, it is evident that axon growth is not only chemical, but mechanosensitive to their environment; revealing a mechanotransduction relationship involving LINC complexes. Recent research has revealed that axons grow faster, straighter, and more parallel on stiffer substrates. Here, we wish to understand the relationship between LAP1 and LINC complexes with varying substrate stiffness to identify TorsinA’s role in mechanotransduction.
Undergraduate Research Symposium | 89