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Assisted Insertion of Pseudomonas aeruginosa Type Three Secretion Translocator PopD in Membranes by Translocator PopB
Author(s) -
Tang Yuzhou,
Heuck Alejandro P.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.815.14
Subject(s) - membrane , secretion , effector , translocon , transmembrane protein , biology , microbiology and biotechnology , inner membrane , cell membrane , pseudomonas aeruginosa , membrane protein , biochemistry , chemistry , bacteria , receptor , genetics
Type III secretion (T3S) system is deployed by a wide range of pathogens to manipulate host cell response and establish infection. The T3S system is a syringe‐like apparatus that spans across the double membrane of bacteria, protruding 40nm–80nm into the extracellular space and connecting with target cell membrane. In Pseudomonas aeruginosa, the proteins PopB and PopD are secreted and found associated with the target eukaryotic cell membrane. These two proteins are believed to form a transmembrane complex or translocon to allow effector protein translocation. We have recently determined that PopD alone can spontaneously oligomerize and form mostly homo‐complexes of six subunits in the membrane. Interestingly, PopB and PopD together form membrane‐inserted hetero‐complexes that contain eight subunits of PopB and eight of PopD. However, the assembly mechanism to form these complexes remains unknown. Here, we investigated how PopD interacts with membranes when assembled into the PopB/D hetero‐complex using a combination of biochemical and biophysical techniques that report on the environment and location of individual amino acid. Our data suggested that the presence of PopB triggers conformational change in membrane associated PopD in lipid bilayers. Using a cell based phosphorylation assay, we also found a similar conformational change of PopD in infected HeLa cell membranes. Together, our results showed that PopB assists the membrane insertion of PopD. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .