Characterizing the Relationship between Eisosomes and Hydrophilins During Desiccation in the Yeast Saccharomyces Cerevisiae

Mariano Bedoya, Jacob Ruiz, and Dr. Hugo Tapia


Due to the impacts of climate change, it has become important to understand how organism react to new changes like the loss of water caused by droughts. Desiccation tolerance is the ability for an organism to survive the loss of intracellular water to as little as 0.1% and when rehydrated the metabolism of the organism resumes normally. Desiccation tolerance biology can lead to a better understanding and possible solutions to many of the problems associated with climate change. A group of proteins that have been shown to play an important role in desiccation tolerance are hydrophilins, characterized by their small size, positive charge and their intrinsically disordered structures. Hydrophilins play a important role in desiccation tolerance through the stabilization of the membranes and proteins during desiccation. Hsp12, the most highly expressed hydrophilin of the desiccation tolerant yeast Saccharomyces cerevisiae, plays a significant role in a variety of stress conditions such as heat shock and has been shown to play a role in the configuration of yeast membranes during stress conditions. Additionally, an uncharacterized hydrophilin, which we will refer to as Dry3 (Desiccation Resistance in Yeast 3), caused a significant decrease in desiccation tolerance when deleted from haploid yeast cells. Therefore, in this study we will use S. cerevisiae as our model organism to further elucidate the role of Hsp12 and Dry3 in desiccation tolerance. We will examine the role of Hsp12 and Dry3 and their possible function as a mediator of the formation and or function of eisosomes (lipid domains in yeast plasma membrane). We are currently working on experiments to co-localize various eisosome components (Pil1-mCherry, Nce102-mCherry) and Hsp12-GFP and Dry3-GFP. We are also currently engineering different strains lacking essential eisosome components (pil1∆ or nce102∆) as well as lacking our hydrophilin genes (hsp12∆, dry3∆) and their different deletion combinations (pil

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