Deciphering the initiation mechanism of Yersinia outer protein secretion
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Bacteria have evolved intricate secretion systems to enhance pathogenicity and
survival, with the Type III Secretion System (T3SS) being a key virulence factor in
many pathogens. This thesis investigates the binding interactions between the
YscXY chaperone-substrate complex and the YscV gate protein in Yersinia,
employing techniques such as protein analysis and cryo-electron microscopy.
Contrary to previous studies, our findings demonstrate that the C-terminal region of
YscX is not essential for binding to YscV, suggesting alternative binding
mechanisms. Additionally, we uncovered significant impacts of storage conditions
on protein oligomerization states, with fresh GST-YscVc displaying a more
complex oligomerization behavior compared to frozen samples. The Δ50 mutation
in YscX promoted higher-order oligomerization, indicating a regulatory role for the
N-terminal region.Cryo-EM analysis achieved a resolution of 2.93 Å, sufficient to
interpret side-chain positions in the rigid regions of the protein. This map provides
detailed structural insights and highlights the importance of specific regions in the
protein complex. Future steps include further refinement of this map and exploring
potential conformational changes during secretion. These insights contribute to a
deeper understanding of T3SS dynamics, offering potential targets for therapeutic
intervention to mitigate bacterial virulence.