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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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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC.
Y. Huang, B. S. Smith, L. X. Chen, R. H. G. Baxter, and J. Deisenhofer (2009)
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Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry.
R. J. Rose, D. Verger, T. Daviter, H. Remaut, E. Paci, G. Waksman, A. E. Ashcroft, and S. E. Radford (2008)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)