Monitoring Activity of Caspases and Their Regulators in Yeast Saccharomyces cerevisiae

Abstract

Caspases are a family of site-specific proteases that play important signaling and effector roles in most apoptotic death pathways. Caspases are made as zymogens and become activated after cleavage. Caspase activity is regulated by both activators and inhibitors. Yeast provide a useful system in which to characterize the function of caspases and their regulators because yeast appear to lack endogenous caspases as well as other components of the apoptotic machinery. Also, yeast are genetically the most tractable eukaryote with which to work. Finally, transformation occurs at a high frequency, making them suitable for library screening or large-scale mutagenesis. In addition to caspases, yeast systems have also been used to analyze other cell death pathway components.2, 3, 4, 5, 6, 7, 8, 9, 10, 11 These approaches are discussed in [27] and [28].