Characterization of Novel Protein Rid1
The fission yeast Schizosaccharomyces pombe is a useful organism in research, providing many experimental advantages including genetic analysis. The organism is unicellular, its genome is the smallest among eukaryotes, and it is highly conserved. These features allow researchers to study biological processes more easily and quickly. Specifically, in our study, the process of cytokinesis. Cytokinesis is a process where a cell divides its cytoplasm to form two daughter cells. Both yeast and animal cells share the mechanism of cytokinesis through an actin-myosin contractile ring, by studying this mechanism we are able to witness one of the key conserved features among eukaryotes. Genomic studies have implicated more than 130 cytokinesis genes in Schizosaccharomyces pombe and many of these genes and their proteins have yet to be characterized. One such protein is Ring-localized protein with homology to Diaphanous GTPase-binding domain (Rid1). This study aims to determine what function, if any, Rid1 has during cytokinesis. First, we tested if the deletion of rid1 affects sensitivity to various stressors. The deletion of rid1 actually helped the cells grow more in two of the stressors, Calcofluor and Latrunculin A. The cells showed a resistance to these stressors that negatively affect the cell’s cytoskeleton and cell wall stability, suggesting Rid1 could be involved in cell wall dynamics and/or cytoskeleton stability during cytokinesis. Future studies will characterize Rid1 cellular localization using florescence microscopy and identify potential interacting partners of Rid1 through large-scale purifications and proteomics; these studies will offer further insight into Rid1’s function.