Abstract
Determination of the substrate specificity of site-specific proteases helps define their physiological roles. We developed a yeast-based system for defining the minimal substrate specificity of site-specific proteases, within the context of a protein. Using this system, we characterized the P4–P1 substrate specificity of the nematode apoptotic caspase CED-3. Apart from an absolute requirement for aspartate at the P1 position, CED-3 is a relatively promiscuous caspase capable of cleaving substrates bearing many amino acids at P4–P2 sites.
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