CAREER: Molecular mechanisms of tardigrade disordered proteins adapted to protect against environmental stress

The project is investigating how tardigrades, a microorganism, mitigate and adapt to the effects of Earth’s changing climate. Tardigrades can survive many environmental extremes, including desiccation, high and low temperatures, radiation, osmotic shock, and pressure. Although the survival mechanisms of tardigrades are poorly understood, evidence points towards accumulation of bioprotectant proteins as a key element to their survival. This research project looks at the structure of several bioprotectant proteins identified in tardigrades and how they protect other proteins when the environment becomes unsuitable for life. Carefully controlled experiments conducted in test tubes and in cultured cells will assist with the interpretation of measurements made directly in living tardigrades. Dr. Davis will advance the state of climate change education in Connecticut and nurture the next generation of interdisciplinary scientists and teachers through a scaffold of education initiatives supported by Yale’s Pathways to Science program. This work will target communities that are most vulnerable to climate impacts. In addition, this proposal will support the training of high school, undergraduate, postgraduate, and graduate researchers on state-of-the-art instrumentation. The research under this award aims to develop a detailed physiochemical understanding of the structure and function of tardigrade disordered proteins. These families of proteins and other intrinsically disordered proteins assist organisms with rapidly adapting to environmental extremes and the goal of this work is to unravel the mechanisms that allow for this. The broad hypothesis is that tardigrade disordered proteins protect other proteins, i.e. prevent aggregation and unfolding, through distinct mechanisms that enable tardigrades to survive extreme stress. In situ infrared and fluorescence imaging techniques are being developed to accomplish two separate but related projects. Optical photothermal infrared imaging will reveal differences in the secondary structure of tardigrade disordered proteins under basal and stress conditions. To determine whether the same structures form in situ, measurements will be made in vitro, in cell, and in living tardigrades. Complementary fast relaxation imaging measurements will examine how tardigrade disordered proteins change the structure and stability of other proteins in vitro and in living tardigrades. Taken together, this proposal will provide insight into the fundamental processes that tardigrades employ to resist climate change and related environmental impacts. This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.