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Type III secretion system mediated secretion and translocation of Yop-effector proteins across the eukaryotic target cell membrane by pathogenic  Yersinia  is highly organized and is dependent on a switching event from secretion of early structural substrates to late effector substrates (Yops). Substrate switching can be mimicked  in vitro  by modulating the calcium levels in the growth medium. YscU that is essential for regulation of this switch undergoes autoproteolysis at a conserved N↑PTH motif, resulting in a 10 kDa C-terminal polypeptide fragment denoted YscU CC . Here we show that depletion of calcium induces intramolecular dissociation of YscU CC  from YscU followed by secretion of the YscU CC  polypeptide. Thus, YscU CC  behaved  in vivo  as a Yop protein with respect to secretion properties. Further, destabilized  ysc U mutants displayed increased rates of dissociation of YscU CC   in vitro  resulting in enhanced Yop secretion  in vivo  at 30°C relative to the wild-type strain.These findings provide strong support to the relevance of YscU CC  dissociation for Yop secretion. We propose that YscU CC  orchestrates a block in the secretion channel that is eliminated by calcium depletion. Further, the striking homology between different members of the YscU/FlhB family suggests that this protein family possess regulatory functions also in other bacteria using comparable mechanisms.

Autoproteolysis and Intramolecular Dissociation of Yersinia YscU Precedes Secretion of Its C-Terminal Polypeptide YscUCC