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Fimbriae are long, adhesive structures widespread throughoutmembers of the family Enterobacteriaceae. They are multimeric extrusions, which are moved out of the bacterial cell through an integral outer membrane protein called usher. The complex folding mechanics of the usher protein were recently revealed to be catalysed by the membrane-embedded translocation and assembly module (TAM). Here, we examine the diversity of usher proteins across a wide range of extraintestinal (ExPEC) and enteropathogenic (EPEC) Escherichia coli, and further focus on a so far undescribed chaperone-usher system, with this usher referred to as UshC. The fimbrial system containing UshCis distributed across a discrete set of EPECtypes, including model strains like E2348/67, as well as ExPEC ST131, currently the most prominent multidrug-resistant uropathogenic E. coli strain worldwide. Deletion of the TAM from a naive strain of E. coli results in a drastic time delay in folding of UshC, which can be observed for a protein from EPEC aswell as for two introduced proteins from related organisms, Yersinia and Enterobacter. We suggest that this models why the TAM machinery is essential for efficient folding of proteins acquired via lateral gene transfer.
- Outer membrane
- Translocation and assembly module
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