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Quantifying Yersinia pseudotuberculosis Type III Secretion System Activity Following Iron Starvation and Anaerobic Growth
Published on: May 31, 2024
SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal
Rasha Younis1, Lewis E H Bingle, Sarah Rollauer
1School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom.
Abstract:
Here we show that the type III secretion gatekeeper protein SepL resembles an aberrant effector protein in binding to a class 1 type III secretion chaperone (Orf12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.
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