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Updated: Jul 5, 2026

Quantifying Yersinia pseudotuberculosis Type III Secretion System Activity Following Iron Starvation and Anaerobic Growth
Published on: May 31, 2024
YscU cleavage and the assembly of Yersinia type III secretion machine complexes
Kelly E Riordan1, Olaf Schneewind
1Department of Microbiology, University of Chicago, Chicago, IL 60637, USA.
Abstract:
YscU, a component of the Yersinia type III secretion machine, promotes auto-cleavage at asparagine 263 (N263). Mutants with an alanine substitution at yscU codon 263 displayed secretion defects for some substrates (LcrV, YopB and YopD); however, transport of effector proteins into host cells (YopE, YopH, YopM) continued to occur. Two yscU mutations were isolated that, unlike N263A, completely abolished type III secretion; YscU(G127D) promoted auto-cleavage at N263, whereas YscU(G270N) did not. When fused to glutathione S-transferase (Gst), the YscU C-terminal cytoplasmic domain promoted auto-cleavage and Gst-YscU(C) also exerted a dominant-negative phenotype by blocking type III secretion. Gst-YscU(C/N263A) caused a similar blockade and Gst-YscU(C/G270N) reduced secretion. Gst-YscU(C) and Gst-YscU(C/N263A) bound YscL, the regulator of the ATPase YscN, whereas Gst-YscU(C/G270N) did not. When isolated from Yersinia, Gst-YscU(C) and Gst-YscU(C/N263A) associated with YscK-YscL-YscQ; however, Gst-YscU(C/G270N) interacted predominantly with the machine component YscO, but not with YscK-YscL-YscQ. A model is proposed whereby YscU auto-cleavage promotes interaction with YscL and recruitment of ATPase complexes that initiate type III secretion.
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