Abstract
The transcription factor Stp1 is endoproteolytically processed in response to extracellular amino acids by the plasma membrane SPS (Ssy1-Ptr3-Ssy5)-sensor. Processed Stp1, lacking a cytoplasmic retention motif, enters the nucleus and induces amino acid transporter gene expression. The SPS-sensor component Ssy5 is a chymotrypsin-like protease with a Pro-domain and a catalytic domain. The Pro-domain, required for protease maturation, is autolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex that binds Stp1. Stp1 is processed only after amino acid-induced signals cause the dissociation of the inhibitory Pro-domain. Our findings demonstrate that gene expression can be controlled by regulating the enzymatic activity of an intracellular endoprotease.
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