Describe your undergraduate research or creative project:
The ParDE4 cassette found in Agrobacterium tumefaciens is of particular interest because it is structurally identical to the Rel-type ribosome-dependent ribonuclease toxin family, but its inhibition of DNA gyrase is indicative of the Par-type toxin family. While it is known that ParE toxin activity results in DNA breaks, either by inhibiting DNA gyrase or by direct nuclease activity, there is a gap in knowledge regarding the specific mechanism(s) of its actions and how this may relate to function. Here, we demonstrate the deoxyribonuclease activity, gyrase inhibition, and translational inhibition activity of toxin. We have also shown that the toxin and antitoxin interact with high picomolar affinity and that the antitoxin does, indeed, neutralize the toxin activity when the two are co-expressed.
Awards and/or presentations:
Ames, Jessica. "Exploration of the Novel Functions of the Bacterial AtParE4 Toxin." Curiosity to Creativity Spring Symposium, 25 April 2018, Oklahoma Memorial Union, Norman, OK.