Cutting, Simon IBN#9418291 University of Pennsylvania An unusually small developmental protein. Spore formation in the gram-positive bacterium Bacillus subtilis represents a simple example of cellular development that has been well characterized morphologically, physiologically and genetically. Interestingly, this prokaryote has certain similarities to development in higher organisms. Most notable is the formation of two cell types during the course of sporulation. These two cell types (of which one is destined to become the spore) are, at first, separated by only two layers of membrane and are thus reminiscent of the compartmentalized structures found in eukaryotic cells, (e.g., mitochondria). Similarly, adjacent daughter cells in a multicullular differentiating organism are separated by only two membrane layers. B. subtilus may be able to serve as a simple model to address how information is communicated throught membranes. In this proposal the structure and function of an extremely small developmental protein, SpoVM, will be determined. The 26 amino acid, 3kD, SpoVM protein is crucial for the development of B. subtilis and is able to interact with phospholipid membranes. The hypothesis is that SpoVM is involved in intercompartmental communication between the mother and daughter cells. This proposal will investigate the nature of the cell-cell communication process and the role that SpoVM may play. The specific aims are: to isolate suppressors of a spoVM mutant, to determine the cellular location of the protein, to determine whether it is an oligomer, to examine its structure by CS spectroscopy and NMR, to carry out liposome binding and channel conductance experiments, to search for interacting proteins, to identify regions of functional importance and to screen for homologues in other spore-forming bacteria.****
