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Updated: Jul 6, 2026

Engineering Adherent Bacteria by Creating a Single Synthetic Curli Operon
Published on: November 16, 2012
Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst
Mireille Nishiyama1, Takashi Ishikawa, Helene Rechsteiner
1Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.
Abstract:
Type 1 pili from uropathogenic Escherichia coli are a prototype of adhesive surface organelles assembled and secreted by the conserved chaperone/usher pathway. We reconstituted type 1 pilus biogenesis from purified pilus proteins. The usher FimD acted as a catalyst to accelerate the ordered assembly of protein subunits independently of cellular energy. Its activity was highly dependent on the adhesin subunit FimH, which triggered the conversion of FimD into a high-efficiency assembly catalyst. Furthermore, a simple kinetic model adequately rationalized usher-catalyzed pilus assembly in vivo. Our results contribute to a mechanistic understanding of protein-catalyzed biogenesis of supramolecular protein complexes at the bacterial outer cell membrane.
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