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Published Online March 27, 2008
Science DOI: 10.1126/science.1154994

Reports

Submitted on January 8, 2008
Accepted on March 18, 2008

Reconstitution of Pilus Assembly Reveals a Bacterial Outer Membrane Catalyst

Mireille Nishiyama 1, Takashi Ishikawa 1, Helene Rechsteiner 1, Rudi Glockshuber 1*

1 Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland

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

Type 1 pili from uropathogenic Escherichia coli are a prototype of adhesive surface organelles assembled and secreted by the conserved chaperone/usher pathway. Here 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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Science. ISSN 0036-8075 (print), 1095-9203 (online)