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Barker, Clive S.; Meshcheryakova, Irina V.; Kostyukova, Alla S.; Samatey, Fadel A. (2010)
Publisher: Public Library of Science
Journal: PLoS Genetics
Languages: English
Types: Article
Subjects: Biophysics/Membrane Proteins and Energy Transduction, Biophysics/Protein Folding, Research Article, Microbiology/Microbial Growth and Development, Biochemistry/Protein Folding, Molecular Biology/Molecular Evolution, QH426-470, Biochemistry/Protein Chemistry, Microbiology/Microbial Physiology and Metabolism, Genetics, Microbiology/Microbial Evolution and Genomics, Biochemistry/Membrane Proteins and Energy Transduction, Genetics and Genomics/Microbial Evolution and Genomics
The type III secretion system of the Salmonella flagellum consists of 6 integral membrane proteins: FlhA, FlhB, FliO, FliP, FliQ, and FliR. However, in some other type III secretion systems, a homologue of FliO is apparently absent, suggesting it has a specialized role. Deleting the fliO gene from the chromosome of a motile strain of Salmonella resulted in a drastic decrease of motility. Incubation of the ΔfliO mutant strain in motility agar, gave rise to pseudorevertants containing extragenic bypass mutations in FliP at positions R143H or F190L. Using membrane topology prediction programs, and alkaline phosphatase or GFPuv chimeric protein fusions into the FliO protein, we demonstrated that FliO is bitopic with its N-terminus in the periplasm and C-terminus in the cytoplasm. Truncation analysis of FliO demonstrated that overexpression of FliO₄₃-₁₂₅ or FliO₁-₉₅ was able to rescue motility of the ΔfliO mutant. Further, residue leucine 91 in the cytoplasmic domain was identified to be important for function. Based on secondary structure prediction, the cytoplasmic domain, FliO₄₃-₁₂₅, should contain beta-structure and alpha-helices. FliO₄₃-₁₂₅-Ala was purified and studied using circular dichroism spectroscopy; however, this domain was disordered, and its structure was a mixture of beta-sheet and random coil. Coexpression of full-length FliO with FliP increased expression levels of FliP, but coexpression with the cytoplasmic domain of FliO did not enhance FliP expression levels. Overexpression of the cytoplasmic domain of FliO further rescued motility of strains deleted for the fliO gene expressing bypass mutations in FliP. These results suggest FliO maintains FliP stability through transmembrane domain interaction. The results also demonstrate that the cytoplasmic domain of FliO has functionality, and it presumably becomes structured while interacting with its binding partners.

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