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Originally published in Science Express on 27 March 2008
Science 18 April 2008:
Vol. 320. no. 5874, pp. 376 - 379
DOI: 10.1126/science.1154994
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Reports

Reconstitution of Pilus Assembly Reveals a Bacterial Outer Membrane Catalyst

Mireille Nishiyama, Takashi Ishikawa, Helene Rechsteiner, Rudi Glockshuber*

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.

Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.

* To whom correspondence should be addressed. E-mail: rudi{at}mol.biol.ethz.ch

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