The essential role of proteases in cellular control mechanisms warrants the identification of the proteases involved. We propose to investigate processes dependent upon protease action in the dimorphic fungus Mucor racemosus by combining biochemical and molecular biological techniques. During spore, swollen spore, and budding yeast-to-hyphal conversions, increases in aminopeptidase as well as carboxypeptidase levels were observed. Preliminary studies indicate that a 39 kilodalton protease (carboxypeptidase; CP2) is expressed in hyphal cells, but not in spore or yeast cells. We propose to isolate and study CP2 by using biochemical and protein chemical methods. The elucidation of the basic biochemistry of CP2 will provide a basis for developing hypotheses about its physiological functions. In addition, these studies should lay the foundation which will lead to our cloning and characterizing the CP2 gene. These investigations should increase the understanding of the relationship of protease to biological control processes in general and could provide information about the control of morphogenesis. These studies, using a fungal model system, are important to our understanding of the growth of this organism. In the long term, these studies have implications for our understanding of protein synthesis and metabolism, and nutrition in many organisms. Protein synthesis, function and transformation is vital in all organisms, yet we know little about the important biochemical events and their regulation. These studies are aimed at increasing our understanding of these important processes.
