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Reference: Pfirrmann T, et al. (2010) The prodomain of ssy5 protease controls receptor-activated proteolysis of transcription factor stp1. Mol Cell Biol 30(13):3299-309

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Abstract


Extracellular amino acids induce the yeast SPS-sensor to endoproteolytically cleave transcription factors Stp1 and Stp2 in a process termed receptor-activated proteolysis (RAP). Ssy5, the activating endoprotease, is synthesized with a large N-terminal Pro-domain and a C-terminal chymotrypsin-like catalytic(Cat)-domain. During biogenesis, Ssy5 cleaves itself, and the Pro- and Cat-domains remain associated forming an inactive primed protease. Here we show that the Pro-domain is a potent inhibitor of Cat-domain activity and that its inactivation is a requisite for RAP. Accordingly, amino acid-induced signals trigger proteasome-dependent degradation of the Pro-domain. A mutation that stabilizes the Pro-domain prevents Stp1 processing, whereas destabilizing mutations lead to constitutive RAP-independent Stp1 processing. We fused a conditional degron to the Pro-domain to synthetically reprogram the amino acid responsive SPS signaling pathway placing it under temperature control. Our results define a regulatory mechanism that is novel for eukaryotic proteases functioning within cells.

Reference Type
Journal Article
Authors
Pfirrmann T, Heessen S, Omnus DJ, Andreasson C, Ljungdahl PO
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